Structural Biochemistry of Microtubules,
Kinesins and their Cargos
Publications
3888256
MIKICA
1
chicago-author-date
50
date
desc
year
14268
https://www.i2bc.paris-saclay.fr/wp-content/plugins/zotpress/
%7B%22status%22%3A%22success%22%2C%22updateneeded%22%3Afalse%2C%22instance%22%3Afalse%2C%22meta%22%3A%7B%22request_last%22%3A0%2C%22request_next%22%3A0%2C%22used_cache%22%3Atrue%7D%2C%22data%22%3A%5B%7B%22key%22%3A%22UZUXMS9H%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Ammar%20Khodja%20et%20al.%22%2C%22parsedDate%22%3A%222024-11%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EAmmar%20Khodja%2C%20Liza%2C%20Val%26%23xE9%3Brie%20Campanacci%2C%20Guy%20Lippens%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202024.%20%26%23x201C%3BThe%20Structure%20of%20a%20Tau%20Fragment%20Bound%20to%20Tubulin%20Prompts%20New%20Hypotheses%20on%20Tau%20Mechanism%20and%20Oligomerization.%26%23x201D%3B%20%3Ci%3EPNAS%20Nexus%3C%5C%2Fi%3E%203%20%2811%29%3A%20pgae487.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1093%5C%2Fpnasnexus%5C%2Fpgae487%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1093%5C%2Fpnasnexus%5C%2Fpgae487%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20structure%20of%20a%20Tau%20fragment%20bound%20to%20tubulin%20prompts%20new%20hypotheses%20on%20Tau%20mechanism%20and%20oligomerization%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Liza%22%2C%22lastName%22%3A%22Ammar%20Khodja%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Guy%22%2C%22lastName%22%3A%22Lippens%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Tau%20is%20a%20protein%20involved%20in%20the%20regulation%20of%20axonal%20microtubules%20in%20neurons.%20In%20pathological%20conditions%2C%20it%20forms%20filamentous%20aggregates%20which%20are%20molecular%20markers%20of%20neurodegenerative%20diseases%20known%20as%20tauopathies.%20Structures%20of%20Tau%20in%20fibrils%20or%20bound%20to%20the%20microtubule%20have%20been%20reported.%20We%20present%20here%20a%20structure%20of%20a%20Tau%20construct%20comprising%20the%20PHF6%20motif%2C%20an%20oligopeptide%20involved%20in%20Tau%20aggregation%2C%20as%20a%20complex%20with%20tubulin.%20This%20Tau%20fragment%20binds%20as%20a%20dimer%20to%20a%20new%20site%20which%2C%20when%20transposed%20to%20the%20microtubule%2C%20would%20correspond%20to%20a%20pore%20between%20protofilaments.%20These%20results%20raise%20new%20hypotheses%20on%20Tau-induced%20microtubule%20assembly%20and%20stabilization%20and%20on%20Tau%20oligomerization.%22%2C%22date%22%3A%222024-11%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1093%5C%2Fpnasnexus%5C%2Fpgae487%22%2C%22ISSN%22%3A%222752-6542%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%5D%2C%22dateModified%22%3A%222024-11-14T08%3A23%3A00Z%22%7D%7D%2C%7B%22key%22%3A%22ADPI5WEY%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Van%20Blerkom%20et%20al.%22%2C%22parsedDate%22%3A%222024-07-06%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EVan%20Blerkom%2C%20Peter%2C%20Armel%20Bezault%2C%20C%26%23xE9%3Bcile%20Sauvanet%2C%20Dorit%20Hanein%2C%20and%20Niels%20Volkmann.%202024.%20%26%23x201C%3BThe%20GoldX%20Fiducial%20Eraser.%26%23x201D%3B%20%3Ci%3EInternational%20Journal%20of%20Molecular%20Sciences%3C%5C%2Fi%3E%2025%20%2813%29%3A%207442.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3390%5C%2Fijms25137442%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3390%5C%2Fijms25137442%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20GoldX%20Fiducial%20Eraser%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Peter%22%2C%22lastName%22%3A%22Van%20Blerkom%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Armel%22%2C%22lastName%22%3A%22Bezault%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22C%5Cu00e9cile%22%2C%22lastName%22%3A%22Sauvanet%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Dorit%22%2C%22lastName%22%3A%22Hanein%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Niels%22%2C%22lastName%22%3A%22Volkmann%22%7D%5D%2C%22abstractNote%22%3A%22Gold%20nanoparticles%20with%20sizes%20in%20the%20range%20of%205-15%20nm%20are%20a%20standard%20method%20of%20providing%20fiducial%20markers%20to%20assist%20with%20alignment%20during%20reconstruction%20in%20cryogenic%20electron%20tomography.%20However%2C%20due%20to%20their%20high%20electron%20density%20and%20resulting%20contrast%20when%20compared%20to%20standard%20cellular%20or%20biological%20samples%2C%20they%20introduce%20artifacts%20such%20as%20streaking%20in%20the%20reconstructed%20tomograms.%20Here%2C%20we%20demonstrate%20a%20tool%20that%20automatically%20detects%20these%20nanoparticles%20and%20suppresses%20them%20by%20replacing%20them%20with%20a%20local%20background%20as%20a%20post-processing%20step%2C%20providing%20a%20cleaner%20tomogram%20without%20removing%20any%20sample%20relevant%20information%20or%20introducing%20new%20artifacts%20or%20edge%20effects%20from%20uniform%20density%20replacements.%22%2C%22date%22%3A%222024-07-06%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.3390%5C%2Fijms25137442%22%2C%22ISSN%22%3A%221422-0067%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%5D%2C%22dateModified%22%3A%222024-07-17T11%3A42%3A13Z%22%7D%7D%2C%7B%22key%22%3A%223BCEZRPC%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Campanacci%20and%20Gigant%22%2C%22parsedDate%22%3A%222023-10-06%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ECampanacci%2C%20Val%26%23xE9%3Brie%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202023.%20%26%23x201C%3BThe%20C-Terminus%20of%20Stathmin-like%20Proteins%20Governs%20the%20Stability%20of%20Their%20Complexes%20with%20Tubulin.%26%23x201D%3B%20%3Ci%3EBiochemical%20and%20Biophysical%20Research%20Communications%3C%5C%2Fi%3E%20682%20%28October%29%3A244%26%23x2013%3B49.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.bbrc.2023.10.023%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.bbrc.2023.10.023%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20C-terminus%20of%20stathmin-like%20proteins%20governs%20the%20stability%20of%20their%20complexes%20with%20tubulin%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Microtubule%20dynamics%20is%20modulated%20by%20many%20cellular%20factors%20including%20stathmin%20family%20proteins.%20Vertebrate%20stathmins%20sequester%20two%20%5Cu03b1%5Cu03b2-tubulin%20heterodimers%20into%20a%20tight%20complex%20that%20cannot%20be%20incorporated%20in%20microtubules.%20Stathmins%20are%20regulated%20at%20the%20expression%20level%20during%20development%20and%20among%20tissues%3B%20they%20are%20also%20regulated%20by%20phosphorylation.%20Here%2C%20we%20study%20the%20dissociation%20kinetics%20of%20tubulin%3Astathmin%20assemblies%20in%20presence%20of%20different%20tubulin-binding%20proteins%20and%20identify%20a%20critical%20role%20of%20the%20C-terminus%20of%20the%20stathmin%20partner.%20Destabilizing%20this%20C-terminal%20region%20may%20represent%20an%20additional%20regulatory%20mechanism%20of%20the%20interaction%20with%20tubulin%20of%20stathmin%20proteins.%22%2C%22date%22%3A%222023-10-06%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.bbrc.2023.10.023%22%2C%22ISSN%22%3A%221090-2104%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%5D%2C%22dateModified%22%3A%222023-10-16T09%3A18%3A02Z%22%7D%7D%2C%7B%22key%22%3A%22SFF9WVN5%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Teixeira-Nunes%20et%20al.%22%2C%22parsedDate%22%3A%222023-09-25%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ETeixeira-Nunes%2C%20Magda%2C%20Pascal%20Retailleau%2C%20Doroth%26%23xE9%3Be%20Raoux-Barbot%2C%20Martine%20Comisso%2C%20Anani%20Amegan%20Missinou%2C%20Christophe%20Velours%2C%20St%26%23xE9%3Bphane%20Plancqueel%2C%20Daniel%20Ladant%2C%20Undine%20Mechold%2C%20and%20Louis%20Renault.%202023.%20%26%23x201C%3BFunctional%20and%20Structural%20Insights%20into%20the%20Multi-Step%20Activation%20and%20Catalytic%20Mechanism%20of%20Bacterial%20ExoY%20Nucleotidyl%20Cyclase%20Toxins%20Bound%20to%20Actin-Profilin.%26%23x201D%3B%20%3Ci%3EPLoS%20Pathogens%3C%5C%2Fi%3E%2019%20%289%29%3A%20e1011654.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1371%5C%2Fjournal.ppat.1011654%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1371%5C%2Fjournal.ppat.1011654%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Functional%20and%20structural%20insights%20into%20the%20multi-step%20activation%20and%20catalytic%20mechanism%20of%20bacterial%20ExoY%20nucleotidyl%20cyclase%20toxins%20bound%20to%20actin-profilin%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magda%22%2C%22lastName%22%3A%22Teixeira-Nunes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Pascal%22%2C%22lastName%22%3A%22Retailleau%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Doroth%5Cu00e9e%22%2C%22lastName%22%3A%22Raoux-Barbot%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Martine%22%2C%22lastName%22%3A%22Comisso%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Anani%20Amegan%22%2C%22lastName%22%3A%22Missinou%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%22%2C%22lastName%22%3A%22Velours%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22St%5Cu00e9phane%22%2C%22lastName%22%3A%22Plancqueel%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daniel%22%2C%22lastName%22%3A%22Ladant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Undine%22%2C%22lastName%22%3A%22Mechold%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Louis%22%2C%22lastName%22%3A%22Renault%22%7D%5D%2C%22abstractNote%22%3A%22ExoY%20virulence%20factors%20are%20members%20of%20a%20family%20of%20bacterial%20nucleotidyl%20cyclases%20%28NCs%29%20that%20are%20activated%20by%20specific%20eukaryotic%20cofactors%20and%20overproduce%20cyclic%20purine%20and%20pyrimidine%20nucleotides%20in%20host%20cells.%20ExoYs%20act%20as%20actin-activated%20NC%20toxins.%20Here%2C%20we%20explore%20the%20Vibrio%20nigripulchritudo%20Multifunctional-Autoprocessing%20Repeats-in-ToXin%20%28MARTX%29%20ExoY%20effector%20domain%20%28Vn-ExoY%29%20as%20a%20model%20for%20ExoY-type%20members%20that%20interact%20with%20monomeric%20%28G-actin%29%20instead%20of%20filamentous%20%28F-actin%29%20actin.%20Vn-ExoY%20exhibits%20moderate%20binding%20affinity%20to%20free%20or%20profilin-bound%20G-actin%20but%20can%20capture%20the%20G-actin%3Aprofilin%20complex%2C%20preventing%20its%20spontaneous%20or%20VASP-%20or%20formin-mediated%20assembly%20at%20F-actin%20barbed%20ends%20in%20vitro.%20This%20mechanism%20may%20prolong%20the%20activated%20cofactor-bound%20state%20of%20Vn-ExoY%20at%20sites%20of%20active%20actin%20cytoskeleton%20remodelling.%20We%20present%20a%20series%20of%20high-resolution%20crystal%20structures%20of%20nucleotide-free%2C%203%27-deoxy-ATP-%20or%203%27-deoxy-CTP-bound%20Vn-ExoY%2C%20activated%20by%20free%20or%20profilin-bound%20G-actin-ATP%5C%2F-ADP%2C%20revealing%20that%20the%20cofactor%20only%20partially%20stabilises%20the%20nucleotide-binding%20pocket%20%28NBP%29%20of%20NC%20toxins.%20Substrate%20binding%20induces%20a%20large%2C%20previously-unidentified%2C%20closure%20of%20their%20NBP%2C%20confining%20catalytically%20important%20residues%20and%20metal%20cofactors%20around%20the%20substrate%2C%20and%20facilitating%20the%20recruitment%20of%20two%20metal%20ions%20to%20tightly%20coordinate%20the%20triphosphate%20moiety%20of%20purine%20or%20pyrimidine%20nucleotide%20substrates.%20We%20validate%20critical%20residues%20for%20both%20the%20purinyl%20and%20pyrimidinyl%20cyclase%20activity%20of%20NC%20toxins%20in%20Vn-ExoY%20and%20its%20distantly-related%20ExoY%20from%20Pseudomonas%20aeruginosa%2C%20which%20specifically%20interacts%20with%20F-actin.%20The%20data%20conclusively%20demonstrate%20that%20NC%20toxins%20employ%20a%20similar%20two-metal-ion%20mechanism%20for%20catalysing%20the%20cyclisation%20of%20nucleotides%20of%20different%20sizes.%20These%20structural%20insights%20into%20the%20dynamics%20of%20the%20actin-binding%20interface%20of%20actin-activated%20ExoYs%20and%20the%20multi-step%20activation%20of%20all%20NC%20toxins%20offer%20new%20perspectives%20for%20the%20specific%20inhibition%20of%20class%20II%20bacterial%20NC%20enzymes.%22%2C%22date%22%3A%222023-09-25%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1371%5C%2Fjournal.ppat.1011654%22%2C%22ISSN%22%3A%221553-7374%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%5D%2C%22dateModified%22%3A%222023-09-27T05%3A40%3A11Z%22%7D%7D%2C%7B%22key%22%3A%22PJYZCDWU%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Teixeira-Nunes%20et%20al.%22%2C%22parsedDate%22%3A%222022-06-16%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ETeixeira-Nunes%2C%20Magda%2C%20Pascal%20Retailleau%2C%20Martine%20Comisso%2C%20Vincent%20Deruelle%2C%20Undine%20Mechold%2C%20and%20Louis%20Renault.%202022.%20%26%23x201C%3BBacterial%20Nucleotidyl%20Cyclases%20Activated%20by%20Calmodulin%20or%20Actin%20in%20Host%20Cells%3A%20Enzyme%20Specificities%20and%20Cytotoxicity%20Mechanisms%20Identified%20to%20Date.%26%23x201D%3B%20%3Ci%3EInternational%20Journal%20of%20Molecular%20Sciences%3C%5C%2Fi%3E%2023%20%2812%29%3A%206743.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3390%5C%2Fijms23126743%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3390%5C%2Fijms23126743%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Bacterial%20Nucleotidyl%20Cyclases%20Activated%20by%20Calmodulin%20or%20Actin%20in%20Host%20Cells%3A%20Enzyme%20Specificities%20and%20Cytotoxicity%20Mechanisms%20Identified%20to%20Date%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magda%22%2C%22lastName%22%3A%22Teixeira-Nunes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Pascal%22%2C%22lastName%22%3A%22Retailleau%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Martine%22%2C%22lastName%22%3A%22Comisso%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Vincent%22%2C%22lastName%22%3A%22Deruelle%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Undine%22%2C%22lastName%22%3A%22Mechold%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Louis%22%2C%22lastName%22%3A%22Renault%22%7D%5D%2C%22abstractNote%22%3A%22Many%20pathogens%20manipulate%20host%20cell%20cAMP%20signaling%20pathways%20to%20promote%20their%20survival%20and%20proliferation.%20Bacterial%20Exoenzyme%20Y%20%28ExoY%29%20toxins%20belong%20to%20a%20family%20of%20invasive%2C%20structurally-related%20bacterial%20nucleotidyl%20cyclases%20%28NC%29.%20Inactive%20in%20bacteria%2C%20they%20use%20proteins%20that%20are%20uniquely%20and%20abundantly%20present%20in%20eukaryotic%20cells%20to%20become%20potent%2C%20unregulated%20NC%20enzymes%20in%20host%20cells.%20Other%20well-known%20members%20of%20the%20family%20include%20Bacillus%20anthracis%20Edema%20Factor%20%28EF%29%20and%20Bordetella%20pertussis%20CyaA.%20Once%20bound%20to%20their%20eukaryotic%20protein%20cofactor%2C%20they%20can%20catalyze%20supra-physiological%20levels%20of%20various%20cyclic%20nucleotide%20monophosphates%20in%20infected%20cells.%20Originally%20identified%20in%20Pseudomonas%20aeruginosa%2C%20ExoY-related%20NC%20toxins%20appear%20now%20to%20be%20more%20widely%20distributed%20among%20various%20%5Cu03b3-%20and%20%5Cu03b2-proteobacteria.%20ExoY-like%20toxins%20represent%20atypical%2C%20poorly%20characterized%20members%20within%20the%20NC%20toxin%20family.%20While%20the%20NC%20catalytic%20domains%20of%20EF%20and%20CyaA%20toxins%20use%20both%20calmodulin%20as%20cofactor%2C%20their%20counterparts%20in%20ExoY-like%20members%20from%20pathogens%20of%20the%20genus%20Pseudomonas%20or%20Vibrio%20use%20actin%20as%20a%20potent%20cofactor%2C%20in%20either%20its%20monomeric%20or%20polymerized%20form.%20This%20is%20an%20original%20subversion%20of%20actin%20for%20cytoskeleton-targeting%20toxins.%20Here%2C%20we%20review%20recent%20advances%20on%20the%20different%20members%20of%20the%20NC%20toxin%20family%20to%20highlight%20their%20common%20and%20distinct%20functional%20characteristics%20at%20the%20molecular%2C%20cytotoxic%20and%20enzymatic%20levels%2C%20and%20important%20aspects%20that%20need%20further%20characterizations.%22%2C%22date%22%3A%222022-06-16%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.3390%5C%2Fijms23126743%22%2C%22ISSN%22%3A%221422-0067%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fwww.mdpi.com%5C%2F1422-0067%5C%2F23%5C%2F12%5C%2F6743%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222022-09-07T13%3A00%3A34Z%22%7D%7D%2C%7B%22key%22%3A%22V8BX8Q9Z%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Campanacci%20et%20al.%22%2C%22parsedDate%22%3A%222022-05-10%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ECampanacci%2C%20Val%26%23xE9%3Brie%2C%20Agathe%20Urvoas%2C%20Liza%20Ammar%20Khodja%2C%20Magali%20Aumont-Nicaise%2C%20Magali%20Noiray%2C%20Sylvie%20Lachkar%2C%20Patrick%20A.%20Curmi%2C%20Philippe%20Minard%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202022.%20%26%23x201C%3BStructural%20Convergence%20for%20Tubulin%20Binding%20of%20CPAP%20and%20Vinca%20Domain%20Microtubule%20Inhibitors.%26%23x201D%3B%20%3Ci%3EProceedings%20of%20the%20National%20Academy%20of%20Sciences%3C%5C%2Fi%3E%20119%20%2819%29%3A%20e2120098119.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.2120098119%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.2120098119%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structural%20convergence%20for%20tubulin%20binding%20of%20CPAP%20and%20vinca%20domain%20microtubule%20inhibitors%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Agathe%22%2C%22lastName%22%3A%22Urvoas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Liza%22%2C%22lastName%22%3A%22Ammar%20Khodja%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Noiray%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sylvie%22%2C%22lastName%22%3A%22Lachkar%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Patrick%20A.%22%2C%22lastName%22%3A%22Curmi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Philippe%22%2C%22lastName%22%3A%22Minard%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222022-05-10%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1073%5C%2Fpnas.2120098119%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fwww.pnas.org%5C%2Fdoi%5C%2Fabs%5C%2F10.1073%5C%2Fpnas.2120098119%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222022-05-12T16%3A28%3A27Z%22%7D%7D%2C%7B%22key%22%3A%229DA8J6T6%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Stein%20et%20al.%22%2C%22parsedDate%22%3A%222022-01-25%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EStein%2C%20Andreas%2C%20Persefoni%20Hilken%20n%26%23xE9%3Be%20Thomopoulou%2C%20Corazon%20Frias%2C%20Sina%20M.%20Hopff%2C%20Paloma%20Varela%2C%20Nicola%20Wilke%2C%20Arul%20Mariappan%2C%20et%20al.%202022.%20%26%23x201C%3BB-nor-Methylene%20Colchicinoid%20PT-100%20Selectively%20Induces%20Apoptosis%20in%20Multidrug-Resistant%20Human%20Cancer%20Cells%20via%20an%20Intrinsic%20Pathway%20in%20a%20Caspase-Independent%20Manner.%26%23x201D%3B%20%3Ci%3EACS%20Omega%3C%5C%2Fi%3E%207%20%283%29%3A%202591%26%23x2013%3B2603.%20%3Ca%20class%3D%27zp-ItemURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1021%5C%2Facsomega.1c04659%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1021%5C%2Facsomega.1c04659%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22B-nor-methylene%20Colchicinoid%20PT-100%20Selectively%20Induces%20Apoptosis%20in%20Multidrug-Resistant%20Human%20Cancer%20Cells%20via%20an%20Intrinsic%20Pathway%20in%20a%20Caspase-Independent%20Manner%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andreas%22%2C%22lastName%22%3A%22Stein%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Persefoni%22%2C%22lastName%22%3A%22Hilken%20n%5Cu00e9e%20Thomopoulou%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Corazon%22%2C%22lastName%22%3A%22Frias%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sina%20M.%22%2C%22lastName%22%3A%22Hopff%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paloma%22%2C%22lastName%22%3A%22Varela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Nicola%22%2C%22lastName%22%3A%22Wilke%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Arul%22%2C%22lastName%22%3A%22Mariappan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J%5Cu00f6rg-Martin%22%2C%22lastName%22%3A%22Neud%5Cu00f6rfl%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexey%20Yu%22%2C%22lastName%22%3A%22Fedorov%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jay%22%2C%22lastName%22%3A%22Gopalakrishnan%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Aram%22%2C%22lastName%22%3A%22Prokop%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hans-G%5Cu00fcnther%22%2C%22lastName%22%3A%22Schmalz%22%7D%5D%2C%22abstractNote%22%3A%22Colchicine%2C%20the%20main%20active%20alkaloid%20from%20Colchicum%20autumnale%20L.%2C%20is%20a%20potent%20tubulin%20binder%20and%20represents%20an%20interesting%20lead%20structure%20for%20the%20development%20of%20potential%20anticancer%20chemotherapeutics.%20We%20report%20on%20the%20synthesis%20and%20investigation%20of%20potentially%20reactive%20colchicinoids%20and%20their%20surprising%20biological%20activities.%20In%20particular%2C%20the%20previously%20undescribed%20colchicinoid%20PT-100%2C%20a%20B-ring%20contracted%206-exo-methylene%20colchicinoid%2C%20exhibits%20extraordinarily%20high%20antiproliferative%20and%20apoptosis-inducing%20effects%20on%20various%20types%20of%20cancer%20cell%20lines%20like%20acute%20lymphoblastic%20leukemia%20%28Nalm6%29%2C%20acute%20myeloid%20leukemia%20%28HL-60%29%2C%20Burkitt-like%20lymphoma%20%28BJAB%29%2C%20human%20melanoma%20%28MelHO%29%2C%20and%20human%20breast%20adenocarcinoma%20%28MCF7%29%20cells%20at%20low%20nanomolar%20concentrations.%20Apoptosis%20induction%20proved%20to%20be%20especially%20high%20in%20multidrug-resistant%20Nalm6-derived%20cancer%20cell%20lines%2C%20while%20healthy%20human%20leukocytes%20and%20hepatocytes%20were%20not%20affected%20by%20the%20concentration%20range%20studied.%20Furthermore%2C%20caspase-independent%20initiation%20of%20apoptosis%20via%20an%20intrinsic%20pathway%20was%20observed.%20PT-100%20also%20shows%20strong%20synergistic%20effects%20in%20combination%20with%20vincristine%20on%20BJAB%20and%20Nalm6%20cells.%20Cocrystallization%20of%20PT-100%20with%20tubulin%20dimers%20revealed%20its%20%28noncovalent%29%20binding%20to%20the%20colchicine-binding%20site%20of%20%5Cu03b2-tubulin%20at%20the%20interface%20to%20the%20%5Cu03b1-subunit.%20A%20pronounced%20effect%20of%20PT-100%20on%20the%20cytoskeleton%20morphology%20was%20shown%20by%20fluorescence%20microscopy.%20While%20the%20reactivity%20of%20PT-100%20as%20a%20weak%20Michael%20acceptor%20toward%20thiols%20was%20chemically%20proven%2C%20it%20remains%20unclear%20whether%20this%20contributes%20to%20the%20remarkable%20biological%20properties%20of%20this%20unusual%20colchicinoid.%22%2C%22date%22%3A%222022-01-25%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1021%5C%2Facsomega.1c04659%22%2C%22ISSN%22%3A%22%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1021%5C%2Facsomega.1c04659%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222022-02-02T14%3A20%3A26Z%22%7D%7D%2C%7B%22key%22%3A%22QN5ZD4P6%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Seul%20et%20al.%22%2C%22parsedDate%22%3A%222021-09-03%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ESeul%2C%20Anait%2C%20Sandrine%20Brasil%26%23xE8%3Bs%2C%20Isabelle%20Petitpas%2C%20Rudi%20Lurz%2C%20Val%26%23xE9%3Brie%20Campanacci%2C%20Christian%20Cambillau%2C%20Frank%20Weise%2C%20Mohamed%20Zairi%2C%20Paulo%20Tavares%2C%20and%20Isabelle%20Auzat.%202021.%20%26%23x201C%3BBiogenesis%20of%20a%20Bacteriophage%20Long%20Non-Contractile%20Tail.%26%23x201D%3B%20%3Ci%3EJournal%20of%20Molecular%20Biology%3C%5C%2Fi%3E%20433%20%2818%29%3A%20167112.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jmb.2021.167112%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.jmb.2021.167112%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Biogenesis%20of%20a%20Bacteriophage%20Long%20Non-Contractile%20Tail%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Anait%22%2C%22lastName%22%3A%22Seul%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sandrine%22%2C%22lastName%22%3A%22Brasil%5Cu00e8s%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Isabelle%22%2C%22lastName%22%3A%22Petitpas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rudi%22%2C%22lastName%22%3A%22Lurz%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christian%22%2C%22lastName%22%3A%22Cambillau%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Frank%22%2C%22lastName%22%3A%22Weise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mohamed%22%2C%22lastName%22%3A%22Zairi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paulo%22%2C%22lastName%22%3A%22Tavares%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Isabelle%22%2C%22lastName%22%3A%22Auzat%22%7D%5D%2C%22abstractNote%22%3A%22Siphoviruses%20are%20main%20killers%20of%20bacteria.%20They%20use%20a%20long%20non-contractile%20tail%20to%20recognize%20the%20host%20cell%20and%20to%20deliver%20the%20genome%20from%20the%20viral%20capsid%20to%20the%20bacterial%20cytoplasm.%20Here%2C%20we%20define%20the%20molecular%20organization%20of%20the%20Bacillus%20subtilis%20bacteriophage%20SPP1%5Cu00a0~%5Cu00a06.8%20MDa%20tail%20and%20uncover%20its%20biogenesis%20mechanisms.%20A%20complex%20between%20gp21%20and%20the%20tail%20distal%20protein%20%28Dit%29%20gp19.1%20is%20assembled%20first%20to%20build%20the%20tail%20cap%20%28gp19.1-gp21Nter%29%20connected%20by%20a%20flexible%20hinge%20to%20the%20tail%20fiber%20%28gp21Cter%29.%20The%20tip%20of%20the%20gp21Cter%20fiber%20is%20loosely%20associated%20to%20gp22.%20The%20cap%20provides%20a%20platform%20where%20tail%20tube%20proteins%20%28TTPs%29%20initiate%20polymerization%20around%20the%20tape%20measure%20protein%20gp18%20%28TMP%29%2C%20a%20reaction%20dependent%20on%20the%20non-structural%20tail%20assembly%20chaperones%20gp17.5%20and%20gp17.5%2A%20%28TACs%29.%20Gp17.5%20is%20essential%20for%20stability%20of%20gp18%20in%20the%20cell.%20Helical%20polymerization%20stops%20at%20a%20precise%20tube%20length%20followed%20by%20binding%20of%20proteins%20gp16.1%20%28TCP%29%20and%20gp17%20%28THJP%29%20to%20build%20the%20tail%20interface%20for%20attachment%20to%20the%20capsid%20portal%20system.%20This%20finding%20uncovers%20the%20function%20of%20the%20extensively%20conserved%20gp16.1-homologs%20in%20assembly%20of%20long%20tails.%20All%20SPP1%20tail%20components%2C%20apart%20from%20gp22%2C%20share%20homology%20to%20conserved%20proteins%20whose%20coding%20genes%27%20synteny%20is%20broadly%20maintained%20in%20siphoviruses.%20They%20conceivably%20represent%20the%20minimal%20essential%20protein%20set%20necessary%20to%20build%20functional%20long%20tails.%20Proteins%20homologous%20to%20SPP1%20tail%20building%20blocks%20feature%20a%20variety%20of%20add-on%20modules%20that%20diversify%20extensively%20the%20tail%20core%20structure%2C%20expanding%20its%20capability%20to%20bind%20host%20cells%20and%20to%20deliver%20the%20viral%20genome%20to%20the%20bacterial%20cytoplasm.%22%2C%22date%22%3A%222021-09-03%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.jmb.2021.167112%22%2C%22ISSN%22%3A%221089-8638%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%2C%22YCWTNSJP%22%5D%2C%22dateModified%22%3A%222021-09-10T13%3A39%3A12Z%22%7D%7D%2C%7B%22key%22%3A%22EFJG8KI5%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Ayukawa%20et%20al.%22%2C%22parsedDate%22%3A%222021-02-05%22%2C%22numChildren%22%3A3%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EAyukawa%2C%20Rie%2C%20Seigo%20Iwata%2C%20Hiroshi%20Imai%2C%20Shinji%20Kamimura%2C%20Masahito%20Hayashi%2C%20Kien%20Xuan%20Ngo%2C%20Itsushi%20Minoura%2C%20et%20al.%202021.%20%26%23x201C%3BGTP-Dependent%20Formation%20of%20Straight%20Tubulin%20Oligomers%20Leads%20to%20Microtubule%20Nucleation.%26%23x201D%3B%20%3Ci%3EJournal%20of%20Cell%20Biology%3C%5C%2Fi%3E%20220%20%28e202007033%29.%20%3Ca%20class%3D%27zp-ItemURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1083%5C%2Fjcb.202007033%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1083%5C%2Fjcb.202007033%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22GTP-dependent%20formation%20of%20straight%20tubulin%20oligomers%20leads%20to%20microtubule%20nucleation%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rie%22%2C%22lastName%22%3A%22Ayukawa%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Seigo%22%2C%22lastName%22%3A%22Iwata%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hiroshi%22%2C%22lastName%22%3A%22Imai%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Shinji%22%2C%22lastName%22%3A%22Kamimura%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Masahito%22%2C%22lastName%22%3A%22Hayashi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kien%20Xuan%22%2C%22lastName%22%3A%22Ngo%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Itsushi%22%2C%22lastName%22%3A%22Minoura%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Seiichi%22%2C%22lastName%22%3A%22Uchimura%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Tsukasa%22%2C%22lastName%22%3A%22Makino%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mikako%22%2C%22lastName%22%3A%22Shirouzu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hideki%22%2C%22lastName%22%3A%22Shigematsu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ken%22%2C%22lastName%22%3A%22Sekimoto%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Etsuko%22%2C%22lastName%22%3A%22Muto%22%7D%5D%2C%22abstractNote%22%3A%22Nucleation%20of%20microtubules%20%28MTs%29%20is%20essential%20for%20cellular%20activities%2C%20but%20its%20mechanism%20is%20unknown%20because%20of%20the%20difficulty%20involved%20in%20capturing%20rare%20stochastic%20events%20in%20the%20early%20stage%20of%20polymerization.%20Here%2C%20combining%20rapid%20flush%20negative%20stain%20electron%20microscopy%20%28EM%29%20and%20kinetic%20analysis%2C%20we%20demonstrate%20that%20the%20formation%20of%20straight%20oligomers%20of%20critical%20size%20is%20essential%20for%20nucleation.%20Both%20GDP%20and%20GTP%20tubulin%20form%20single-stranded%20oligomers%20with%20a%20broad%20range%20of%20curvatures%2C%20but%20upon%20nucleation%2C%20the%20curvature%20distribution%20of%20GTP%20oligomers%20is%20shifted%20to%20produce%20a%20minor%20population%20of%20straight%20oligomers.%20With%20tubulin%20having%20the%20Y222F%20mutation%20in%20the%20%5Cu03b2%20subunit%2C%20the%20proportion%20of%20straight%20oligomers%20increases%20and%20nucleation%20accelerates.%20Our%20results%20support%20a%20model%20in%20which%20GTP%20binding%20generates%20a%20minor%20population%20of%20straight%20oligomers%20compatible%20with%20lateral%20association%20and%20further%20growth%20to%20MTs.%20This%20study%20suggests%20that%20cellular%20factors%20involved%20in%20nucleation%20promote%20it%20via%20stabilization%20of%20straight%20oligomers.%22%2C%22date%22%3A%22February%205%2C%202021%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1083%5C%2Fjcb.202007033%22%2C%22ISSN%22%3A%220021-9525%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1083%5C%2Fjcb.202007033%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222021-02-15T09%3A01%3A39Z%22%7D%7D%2C%7B%22key%22%3A%22HTRTAYCK%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Varela%20et%20al.%22%2C%22parsedDate%22%3A%222021-01-29%22%2C%22numChildren%22%3A3%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EVarela%2C%20Paloma%20F.%2C%20M%26%23xE9%3Blanie%20Chenon%2C%20Christophe%20Velours%2C%20Kristen%20J.%20Verhey%2C%20Julie%20M%26%23xE9%3Bn%26%23xE9%3Btrey%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202021.%20%26%23x201C%3BStructural%20Snapshots%20of%20the%20Kinesin-2%20OSM-3%20along%20Its%20Nucleotide%20Cycle%3A%20Implications%20for%20the%20ATP%20Hydrolysis%20Mechanism.%26%23x201D%3B%20%3Ci%3EFEBS%20Open%20Bio%3C%5C%2Fi%3E%2011%20%283%29%3A%20564%26%23x2013%3B77.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1002%5C%2F2211-5463.13101%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1002%5C%2F2211-5463.13101%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structural%20snapshots%20of%20the%20kinesin-2%20OSM-3%20along%20its%20nucleotide%20cycle%3A%20implications%20for%20the%20ATP%20hydrolysis%20mechanism%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paloma%20F.%22%2C%22lastName%22%3A%22Varela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M%5Cu00e9lanie%22%2C%22lastName%22%3A%22Chenon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%22%2C%22lastName%22%3A%22Velours%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Kristen%20J.%22%2C%22lastName%22%3A%22Verhey%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Julie%22%2C%22lastName%22%3A%22M%5Cu00e9n%5Cu00e9trey%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Motile%20kinesins%20are%20motor%20proteins%20that%20translocate%20along%20microtubules%20as%20they%20hydrolyze%20ATP.%20They%20share%20a%20conserved%20motor%20domain%20which%20harbors%20both%20ATPase%20and%20microtubule-binding%20activities.%20An%20ATP%20hydrolysis%20mechanism%20involving%20two%20water%20molecules%20has%20been%20proposed%20based%20on%20the%20structure%20of%20the%20kinesin-5%20Eg5%20bound%20to%20an%20ATP%20analog.%20Whether%20this%20mechanism%20is%20general%20in%20the%20kinesin%20superfamily%20remains%20uncertain.%20Here%2C%20we%20present%20structural%20snapshots%20of%20the%20motor%20domain%20of%20OSM-3%20along%20its%20nucleotide%20cycle.%20OSM-3%20belongs%20to%20the%20homodimeric%20kinesin-2%20subfamily%20and%20is%20the%20Caenorhabditis%5Cu00a0elegans%20homologue%20of%20human%20KIF17.%20OSM-3%20bound%20to%20ADP%20or%20devoid%20of%20a%20nucleotide%20shows%20features%20of%20ADP-kinesins%20with%20a%20docked%20neck%20linker.%20When%20bound%20to%20an%20ATP%20analog%2C%20OSM-3%20adopts%20a%20conformation%20similar%20to%20those%20of%20several%20ATP-like%20kinesins%2C%20either%20isolated%20or%20bound%20to%20tubulin.%20Moreover%2C%20the%20OSM-3%20nucleotide-binding%20site%20is%20virtually%20identical%20to%20that%20of%20ATP-like%20Eg5%2C%20demonstrating%20a%20shared%20ATPase%20mechanism.%20Therefore%2C%20our%20data%20extend%20to%20kinesin-2%20the%20two-water%20ATP%20hydrolysis%20mechanism%20and%20further%20suggest%20that%20it%20is%20universal%20within%20the%20kinesin%20superfamily.%20PROTEIN%20DATABASE%20ENTRIES%3A%207A3Z%2C%207A40%2C%207A5E.%22%2C%22date%22%3A%222021-01-29%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1002%5C%2F2211-5463.13101%22%2C%22ISSN%22%3A%222211-5463%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222022-06-07T12%3A21%3A42Z%22%7D%7D%2C%7B%22key%22%3A%22L88GE3BQ%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Silistre%20et%20al.%22%2C%22parsedDate%22%3A%222021%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ESilistre%2C%20Hazel%2C%20Doroth%26%23xE9%3Be%20Raoux-Barbot%2C%20Federica%20Mancinelli%2C%20Flora%20Sangouard%2C%20Alice%20Dupin%2C%20Alexander%20Belyy%2C%20Vincent%20Deruelle%2C%20et%20al.%202021.%20%26%23x201C%3BPrevalence%20of%20ExoY%20Activity%20in%20Pseudomonas%20Aeruginosa%20Reference%20Panel%20Strains%20and%20Impact%20on%20Cytotoxicity%20in%20Epithelial%20Cells.%26%23x201D%3B%20%3Ci%3EFrontiers%20in%20Microbiology%3C%5C%2Fi%3E%2012%3A666097.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3389%5C%2Ffmicb.2021.666097%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3389%5C%2Ffmicb.2021.666097%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Prevalence%20of%20ExoY%20Activity%20in%20Pseudomonas%20aeruginosa%20Reference%20Panel%20Strains%20and%20Impact%20on%20Cytotoxicity%20in%20Epithelial%20Cells%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hazel%22%2C%22lastName%22%3A%22Silistre%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Doroth%5Cu00e9e%22%2C%22lastName%22%3A%22Raoux-Barbot%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Federica%22%2C%22lastName%22%3A%22Mancinelli%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Flora%22%2C%22lastName%22%3A%22Sangouard%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alice%22%2C%22lastName%22%3A%22Dupin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexander%22%2C%22lastName%22%3A%22Belyy%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Vincent%22%2C%22lastName%22%3A%22Deruelle%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Louis%22%2C%22lastName%22%3A%22Renault%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daniel%22%2C%22lastName%22%3A%22Ladant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Lhousseine%22%2C%22lastName%22%3A%22Touqui%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Undine%22%2C%22lastName%22%3A%22Mechold%22%7D%5D%2C%22abstractNote%22%3A%22ExoY%20is%20among%20the%20effectors%20that%20are%20injected%20by%20the%20type%20III%20secretion%20system%20%28T3SS%29%20of%20Pseudomonas%20aeruginosa%20into%20host%20cells.%20Inside%20eukaryotic%20cells%2C%20ExoY%20interacts%20with%20F-actin%2C%20which%20stimulates%20its%20potent%20nucleotidyl%20cyclase%20activity%20to%20produce%20cyclic%20nucleotide%20monophosphates%20%28cNMPs%29.%20ExoY%20has%20broad%20substrate%20specificity%20with%20GTP%20as%20a%20preferential%20substrate%20in%20vitro.%20How%20ExoY%20contributes%20to%20the%20virulence%20of%20P.%20aeruginosa%20remains%20largely%20unknown.%20Here%2C%20we%20examined%20the%20prevalence%20of%20active%20ExoY%20among%20strains%20from%20the%20international%20P.%20aeruginosa%20reference%20panel%2C%20a%20collection%20of%20strains%20that%20includes%20environmental%20and%20clinical%20isolates%2C%20commonly%20used%20laboratory%20strains%2C%20and%20sequential%20clonal%20isolates%20from%20cystic%20fibrosis%20%28CF%29%20patients%20and%20thus%20represents%20the%20large%20diversity%20of%20this%20bacterial%20species.%20The%20ability%20to%20secrete%20active%20ExoY%20was%20determined%20by%20measuring%20the%20F-actin%20stimulated%20guanylate%20cyclase%20%28GC%29%20activity%20in%20bacterial%20culture%20supernatants.%20We%20found%20an%20overall%20ExoY%20activity%20prevalence%20of%20about%2060%25%20among%20the%2040%20examined%20strains%20with%20no%20significant%20difference%20between%20CF%20and%20non-CF%20isolates.%20In%20parallel%2C%20we%20used%20cellular%20infection%20models%20of%20human%20lung%20epithelial%20cells%20to%20compare%20the%20cytotoxic%20effects%20of%20isogenic%20reference%20strains%20expressing%20active%20ExoY%20or%20lacking%20the%20exoY%20gene.%20We%20found%20that%20P.%20aeruginosa%20strains%20lacking%20ExoY%20were%20in%20fact%20more%20cytotoxic%20to%20the%20epithelial%20cells%20than%20those%20secreting%20active%20ExoY.%20This%20suggests%20that%20under%20certain%20conditions%2C%20ExoY%20might%20partly%20alleviate%20the%20cytotoxic%20effects%20of%20other%20virulence%20factors%20of%20P.%20aeruginosa.%22%2C%22date%22%3A%222021%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.3389%5C%2Ffmicb.2021.666097%22%2C%22ISSN%22%3A%221664-302X%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222021-10-27T13%3A12%3A51Z%22%7D%7D%2C%7B%22key%22%3A%22ZTTBDI9I%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Shchegravina%20et%20al.%22%2C%22parsedDate%22%3A%222020-12-01%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EShchegravina%2C%20Ekaterina%20S.%2C%20Elena%20V.%20Svirshchevskaya%2C%20Sebastien%20Combes%2C%20Diane%20Allegro%2C%20Pascale%20Barbier%2C%20Benoit%20Gigant%2C%20Paloma%20F.%20Varela%2C%20et%20al.%202020.%20%26%23x201C%3BDiscovery%20of%20Dihydrofuranoallocolchicinoids%20-%20Highly%20Potent%20Antimitotic%20Agents%20with%20Low%20Acute%20Toxicity.%26%23x201D%3B%20%3Ci%3EEuropean%20Journal%20of%20Medicinal%20Chemistry%3C%5C%2Fi%3E%20207%20%28December%29%3A112724.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.ejmech.2020.112724%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.ejmech.2020.112724%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Discovery%20of%20dihydrofuranoallocolchicinoids%20-%20Highly%20potent%20antimitotic%20agents%20with%20low%20acute%20toxicity%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ekaterina%20S.%22%2C%22lastName%22%3A%22Shchegravina%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Elena%20V.%22%2C%22lastName%22%3A%22Svirshchevskaya%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Sebastien%22%2C%22lastName%22%3A%22Combes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Diane%22%2C%22lastName%22%3A%22Allegro%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Pascale%22%2C%22lastName%22%3A%22Barbier%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Benoit%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paloma%20F.%22%2C%22lastName%22%3A%22Varela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrei%20E.%22%2C%22lastName%22%3A%22Gavryushin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Daria%20A.%22%2C%22lastName%22%3A%22Kobanova%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andrey%20E.%22%2C%22lastName%22%3A%22Shchekotikhin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexey%20Yu%22%2C%22lastName%22%3A%22Fedorov%22%7D%5D%2C%22abstractNote%22%3A%22Two%20series%20of%20heterocyclic%20colchicinoids%20bearing%20%5Cu03b2-methylenedihydrofuran%20or%202H-pyran-2-one%20fragments%20were%20synthesized%20by%20the%20intramolecular%20Heck%20reaction.%20Methylenedihydrofuran%20compounds%209a%20and%209h%20were%20found%20to%20be%20the%20most%20cytotoxic%20among%20currently%20known%20colchicinoids%2C%20exhibiting%20outstanding%20antiproliferative%20activity%20on%20tumor%20cell%20lines%20in%20picomolar%20%280.01%5Cu20132.1%5Cu00a0nM%29%20range%20of%20concentrations.%20Compound%209a%20potently%20and%20substoichiometrically%20inhibits%20microtubule%20formation%20in%5Cu00a0vitro%2C%20being%20an%20order%20of%20magnitude%20more%20active%20in%20this%20assay%20than%20colchicine.%20Derivatives%209a%20and%209h%20revealed%20relatively%20low%20acute%20toxicity%20in%20mice%20%28LD50%5Cu00a0%5Cu2265%5Cu00a010%5Cu00a0mg%5C%2Fkg%20i.v.%29.%20The%20X-Ray%20structure%20of%20colchicinoid%209a%20bound%20to%20tubulin%20confirmed%20interaction%20of%20this%20compound%20with%20the%20colchicine%20binding%20site%20of%20tubulin.%22%2C%22date%22%3A%222020-12-01%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.ejmech.2020.112724%22%2C%22ISSN%22%3A%220223-5234%22%2C%22url%22%3A%22https%3A%5C%2F%5C%2Fwww.sciencedirect.com%5C%2Fscience%5C%2Farticle%5C%2Fpii%5C%2FS0223523420306966%22%2C%22collections%22%3A%5B%227EGDQ8LV%22%2C%22A2CFXNDW%22%5D%2C%22dateModified%22%3A%222023-01-25T12%3A04%3A48Z%22%7D%7D%2C%7B%22key%22%3A%22AK728UNR%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Knossow%20et%20al.%22%2C%22parsedDate%22%3A%222020-08-29%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EKnossow%2C%20Marcel%2C%20Val%26%23xE9%3Brie%20Campanacci%2C%20Liza%20Ammar%20Khodja%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202020.%20%26%23x201C%3BThe%20Mechanism%20of%20Tubulin%20Assembly%20into%20Microtubules%3A%20Insights%20from%20Structural%20Studies.%26%23x201D%3B%20%3Ci%3EIScience%3C%5C%2Fi%3E%2023%20%289%29%3A%20101511.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.isci.2020.101511%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.isci.2020.101511%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20Mechanism%20of%20Tubulin%20Assembly%20into%20Microtubules%3A%20Insights%20from%20Structural%20Studies%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marcel%22%2C%22lastName%22%3A%22Knossow%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Liza%20Ammar%22%2C%22lastName%22%3A%22Khodja%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Microtubules%20are%20cytoskeletal%20components%20involved%20in%20pivotal%20eukaryotic%20functions%20such%20as%20cell%20division%2C%20ciliogenesis%2C%20and%20intracellular%20trafficking.%20They%20assemble%20from%20%5Cu03b1%5Cu03b2-tubulin%20heterodimers%20and%20disassemble%20in%20a%20process%20called%20dynamic%20instability%2C%20which%20is%20driven%20by%20GTP%20hydrolysis.%20Structures%20of%20the%20microtubule%20and%20of%20soluble%20tubulin%20have%20been%20determined%20by%20cryo-EM%20and%20by%20X-ray%20crystallography%2C%20respectively.%20Altogether%2C%20these%20data%20define%20the%20mechanism%20of%20tubulin%20assembly-disassembly%20at%20atomic%20or%20near-atomic%20level.%20We%20review%20here%20the%20structural%20changes%20that%20occur%20during%20assembly%2C%20tubulin%20switching%20from%20a%20curved%20conformation%20in%20solution%20to%20a%20straight%20one%20in%20the%20microtubule%20core.%20We%20also%20present%20more%20subtle%20changes%20associated%20with%20GTP%20binding%2C%20leading%20to%20tubulin%20activation%20for%20assembly.%20Finally%2C%20we%20show%20how%20cryo-EM%20and%20X-ray%20crystallography%20are%20complementary%20methods%20to%20characterize%20the%20interaction%20of%20tubulin%20with%20proteins%20involved%20either%20in%20intracellular%20transport%20or%20in%20microtubule%20dynamics%20regulation.%22%2C%22date%22%3A%22Aug%2029%2C%202020%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.isci.2020.101511%22%2C%22ISSN%22%3A%222589-0042%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222021-01-04T14%3A52%3A37Z%22%7D%7D%2C%7B%22key%22%3A%22SDPKGQ72%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Vilela%20et%20al.%22%2C%22parsedDate%22%3A%222019-11-05%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EVilela%2C%20Fernando%2C%20Christophe%20Velours%2C%20M%26%23xE9%3Blanie%20Chenon%2C%20Magali%20Aumont-Nicaise%2C%20Val%26%23xE9%3Brie%20Campanacci%2C%20Aur%26%23xE9%3Blien%20Thureau%2C%20Olena%20Pylypenko%2C%20Jessica%20Andreani%2C%20Paola%20Llinas%2C%20and%20Julie%20M%26%23xE9%3Bn%26%23xE9%3Btrey.%202019.%20%26%23x201C%3BStructural%20Characterization%20of%20the%20RH1-LZI%20Tandem%20of%20JIP3%5C%2F4%20Highlights%20RH1%20Domains%20as%20a%20Cytoskeletal%20Motor-Binding%20Motif.%26%23x201D%3B%20%3Ci%3EScientific%20Reports%3C%5C%2Fi%3E%209%20%281%29%3A%2016036.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41598-019-52537-3%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41598-019-52537-3%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structural%20characterization%20of%20the%20RH1-LZI%20tandem%20of%20JIP3%5C%2F4%20highlights%20RH1%20domains%20as%20a%20cytoskeletal%20motor-binding%20motif%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Fernando%22%2C%22lastName%22%3A%22Vilela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%22%2C%22lastName%22%3A%22Velours%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M%5Cu00e9lanie%22%2C%22lastName%22%3A%22Chenon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Aur%5Cu00e9lien%22%2C%22lastName%22%3A%22Thureau%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Olena%22%2C%22lastName%22%3A%22Pylypenko%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jessica%22%2C%22lastName%22%3A%22Andreani%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paola%22%2C%22lastName%22%3A%22Llinas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Julie%22%2C%22lastName%22%3A%22M%5Cu00e9n%5Cu00e9trey%22%7D%5D%2C%22abstractNote%22%3A%22JIP3%20and%20JIP4%20%28JNK-interacting%20proteins%203%20and%204%29%20are%20adaptors%20for%20cargo%20recruitment%20by%20dynein%5C%2Fdynactin%20and%20kinesin1%20motors.%20Both%20are%20dimers%20that%20are%20stabilised%20by%20two%20sections%20of%20leucine%20zipper%20coiled%20coils.%20The%20N-terminal%20Leucine%20Zipper%20I%20%28LZI%29%20belongs%20to%20a%20section%20that%20binds%20dynein-DLIC%20and%20kinesin1-KHC%2C%20whilst%20the%20medial%20Leucine%20Zipper%20II%20%28LZII%29%20binds%20dynactin-p150glued%20and%20kinesin1-KLC.%20Structural%20data%20is%20available%20for%20the%20LZII%2C%20but%20the%20LZI%20section%20is%20still%20uncharacterized.%20Here%20we%20characterize%20the%20N-terminal%20part%20of%20JIP3%5C%2F4%20which%20consists%20of%20an%20RH1%20%28RILP%20homology%201%29%20domain%20followed%20by%20the%20LZI%20coiled%20coil%20using%20bioinformatical%2C%20biophysical%20and%20structural%20approaches.%20The%20RH1-LZI%20tandem%20of%20JIP3%20associates%20as%20a%20high%20affinity%20homodimer%20exhibiting%20elongated%20alpha-helical%20fold.%203D%20homology%20modelling%20of%20the%20RH1-LZI%20tandem%20reveals%20that%20the%20kinesin1-KHC%20binding%20site%20mainly%20overlaps%20with%20the%20RH1%20domain.%20A%20sequence%20comparison%20search%20indicates%20that%20only%20one%20other%20protein%20family%20has%20RH1%20domains%20similar%20to%20those%20of%20JIP3%5C%2F4%2C%20the%20RILP%20%28Rab-interacting%20lysosomal%20protein%29%20family%20which%20consists%20of%20adaptor%20proteins%20linking%20Rab%20GTPases%20to%20cytoskeletal%20motors.%20RILPL2%20is%20recruited%20through%20its%20RH1%20domain%20by%20the%20myosin%205a%20motor.%20Here%2C%20we%20showed%20that%20the%20RH1%20domain%20of%20JIP3%20also%20interacts%20with%20myosin%205%5Cu2009A%20in%20vitro%2C%20highlighting%20JIP3%5C%2F4%20as%20possible%20myosin%205a%20adaptors.%20Finally%2C%20we%20propose%20that%20JIP3%5C%2F4%20and%20RILP%20family%20members%20define%20a%20unique%20RH1%5C%2FRH2-architecture%20adaptor%20superfamily%20linking%20cytoskeletal%20motors%20and%20Rab%20GTPases.%22%2C%22date%22%3A%22Nov%2005%2C%202019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fs41598-019-52537-3%22%2C%22ISSN%22%3A%222045-2322%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222019-12-23T14%3A30%3A42Z%22%7D%7D%2C%7B%22key%22%3A%22RVL7ZAYK%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Lippens%20and%20Gigant%22%2C%22parsedDate%22%3A%222019-05-14%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELippens%2C%20Guy%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202019.%20%26%23x201C%3BElucidating%20Tau%20Function%20and%20Dysfunction%20in%20the%20Era%20of%20Cryo-EM.%26%23x201D%3B%20%3Ci%3EThe%20Journal%20of%20Biological%20Chemistry%3C%5C%2Fi%3E%20294%20%2824%29%3A%209316%26%23x2013%3B25.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1074%5C%2Fjbc.REV119.008031%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1074%5C%2Fjbc.REV119.008031%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Elucidating%20Tau%20function%20and%20dysfunction%20in%20the%20era%20of%20cryo-EM%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Guy%22%2C%22lastName%22%3A%22Lippens%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Tau%20is%20a%20microtubule-associated%20protein%20involved%20in%20the%20regulation%20of%20axonal%20microtubules%20in%20neurons.%20In%20pathological%20conditions%2C%20it%20forms%20fibrils%20that%20are%20molecular%20hallmarks%20of%20neurological%20disorders%20known%20as%20tauopathies.%20In%20the%20last%20two%20years%2C%20cryo-EM%20has%20given%20unprecedented%20high-resolution%20views%20of%20Tau%20in%20both%20physiological%20and%20pathological%20conditions.%20We%20review%20here%20these%20new%20findings%20and%20put%20them%20into%20the%20context%20of%20the%20knowledge%20about%20Tau%20before%20this%20structural%20breakthrough.%20The%20first%20structures%20of%20Tau%20fibrils%2C%20a%20molecular%20hallmark%20of%20Alzheimer%27s%20disease%20%28AD%29%2C%20were%20based%20on%20fibrils%20from%20the%20brain%20of%20an%20individual%20with%20AD%20and%2C%20along%20with%20similar%20patient-derived%20structures%2C%20have%20set%20the%20gold%20standard%20for%20the%20field.%20Cryo-EM%20structures%20of%20Tau%20fibers%20in%20three%20distinct%20diseases%2C%20AD%2C%20Pick%27s%20disease%20and%20Chronic%20Traumatic%20Encephalopathy%2C%20represent%20the%20end-points%20of%20Tau%27s%20molecular%20trajectory.%20We%20propose%20that%20the%20recent%20Tau%20structures%20may%20call%20for%20a%20re-examination%20of%20databases%20that%20link%20different%20Tau%20variants%20to%20various%20forms%20of%20dementia.%20We%20also%20address%20the%20question%20how%20this%20structural%20information%20may%20link%20Tau%27s%20functional%20and%20pathological%20aspects.%20Because%20this%20structural%20information%20on%20Tau%20was%20obtained%20in%20a%20very%20short%20period%2C%20the%20new%20structures%20should%20be%20viewed%20in%20light%20of%20earlier%20structural%20observations%20and%20past%20and%20present%20functional%20data%20to%20shed%20additional%20light%20on%20Tau%20function%20and%20dysfunction.%22%2C%22date%22%3A%22May%2014%2C%202019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1074%5C%2Fjbc.REV119.008031%22%2C%22ISSN%22%3A%221083-351X%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222023-12-14T15%3A38%3A02Z%22%7D%7D%2C%7B%22key%22%3A%226TGE8EAT%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Campanacci%20et%20al.%22%2C%22parsedDate%22%3A%222019-04-29%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ECampanacci%2C%20Val%26%23xE9%3Brie%2C%20Agathe%20Urvoas%2C%20Soraya%20Cantos-Fernandes%2C%20Magali%20Aumont-Nicaise%2C%20Ana-Andreea%20Arteni%2C%20Christophe%20Velours%2C%20Marie%20Valerio-Lepiniec%2C%20et%20al.%202019.%20%26%23x201C%3BInsight%20into%20Microtubule%20Nucleation%20from%20Tubulin-Capping%20Proteins.%26%23x201D%3B%20%3Ci%3EProceedings%20of%20the%20National%20Academy%20of%20Sciences%20of%20the%20United%20States%20of%20America%3C%5C%2Fi%3E%20116%20%2820%29%3A%209859%26%23x2013%3B64.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1813559116%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1073%5C%2Fpnas.1813559116%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Insight%20into%20microtubule%20nucleation%20from%20tubulin-capping%20proteins%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Agathe%22%2C%22lastName%22%3A%22Urvoas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Soraya%22%2C%22lastName%22%3A%22Cantos-Fernandes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ana-Andreea%22%2C%22lastName%22%3A%22Arteni%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%22%2C%22lastName%22%3A%22Velours%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marie%22%2C%22lastName%22%3A%22Valerio-Lepiniec%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Birgit%22%2C%22lastName%22%3A%22Dreier%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andreas%22%2C%22lastName%22%3A%22Pl%5Cu00fcckthun%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Antoine%22%2C%22lastName%22%3A%22Pilon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christian%22%2C%22lastName%22%3A%22Po%5Cu00fcs%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Philippe%22%2C%22lastName%22%3A%22Minard%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Nucleation%20is%20one%20of%20the%20least%20understood%20steps%20of%20microtubule%20dynamics.%20It%20is%20a%20kinetically%20unfavorable%20process%20that%20is%20templated%20in%20the%20cell%20by%20the%20%5Cu03b3-tubulin%20ring%20complex%20or%20by%20preexisting%20microtubules%3B%20it%20also%20occurs%20in%20vitro%20from%20pure%20tubulin.%20Here%20we%20study%20the%20nucleation%20inhibition%20potency%20of%20natural%20or%20artificial%20proteins%20in%20connection%20with%20their%20binding%20mode%20to%20the%20longitudinal%20surface%20of%20%5Cu03b1-%20or%20%5Cu03b2-tubulin.%20The%20structure%20of%20tubulin-bound%20CopN%2C%20a%20Chlamydia%20protein%20that%20delays%20nucleation%2C%20suggests%20that%20this%20protein%20may%20interfere%20with%20two%20protofilaments%20at%20the%20%28%2B%29%20end%20of%20a%20nucleus.%20Designed%20ankyrin%20repeat%20proteins%20that%20share%20a%20binding%20mode%20similar%20to%20that%20of%20CopN%20also%20impede%20nucleation%2C%20whereas%20those%20that%20target%20only%20one%20protofilament%20do%20not.%20In%20addition%2C%20an%20%5Cu03b1Rep%20protein%20predicted%20to%20target%20two%20protofilaments%20at%20the%20%28-%29%20end%20does%20not%20delay%20nucleation%2C%20pointing%20to%20different%20behaviors%20at%20both%20ends%20of%20the%20nucleus.%20Our%20results%20link%20the%20interference%20with%20protofilaments%20at%20the%20%28%2B%29%20end%20and%20the%20inhibition%20of%20nucleation.%22%2C%22date%22%3A%22Apr%2029%2C%202019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1073%5C%2Fpnas.1813559116%22%2C%22ISSN%22%3A%221091-6490%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222023-12-14T15%3A34%3A36Z%22%7D%7D%2C%7B%22key%22%3A%222BCDTWT4%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Campanacci%20et%20al.%22%2C%22parsedDate%22%3A%222019-03-05%22%2C%22numChildren%22%3A1%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ECampanacci%2C%20Valerie%2C%20Agathe%20Urvoas%2C%20Tanja%20Consolati%2C%20Soraya%20Cantos-Fernandes%2C%20Magali%20Aumont-Nicaise%2C%20Marie%20Valerio-Lepiniec%2C%20Thomas%20Surrey%2C%20Philippe%20Minard%2C%20and%20Benoit%20Gigant.%202019.%20%26%23x201C%3BSelection%20and%20Characterization%20of%20Artificial%20Proteins%20Targeting%20the%20Tubulin%20Alpha%20Subunit.%26%23x201D%3B%20%3Ci%3EStructure%3C%5C%2Fi%3E%2027%20%283%29%3A%20497%26%23x2013%3B506.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.str.2018.12.001%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.str.2018.12.001%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Selection%20and%20Characterization%20of%20Artificial%20Proteins%20Targeting%20the%20Tubulin%20alpha%20Subunit%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Valerie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Agathe%22%2C%22lastName%22%3A%22Urvoas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Tanja%22%2C%22lastName%22%3A%22Consolati%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Soraya%22%2C%22lastName%22%3A%22Cantos-Fernandes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marie%22%2C%22lastName%22%3A%22Valerio-Lepiniec%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Thomas%22%2C%22lastName%22%3A%22Surrey%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Philippe%22%2C%22lastName%22%3A%22Minard%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Benoit%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Microtubules%20are%20cytoskeletal%20filaments%20of%20eukaryotic%20cells%20made%20of%20alpha%20beta-tubulin%20heterodimers.%20Structural%20studies%20of%20non-microtubular%20tubulin%20rely%20mainly%20on%20molecules%20that%20prevent%20its%20self-assembly%20and%20are%20used%20as%20crystallization%20chaperones.%20Here%20we%20identified%20artificial%20proteins%20from%20an%20alpha%20Rep%20library%20that%20are%20specific%20to%20alpha-tubulin.%20Turbidity%20experiments%20indicate%20that%20these%20alpha%20Reps%20impede%20microtubule%20assembly%20in%20a%20dose-dependent%20manner%20and%20total%20internal%20reflection%20fluorescence%20microscopy%20further%20shows%20that%20they%20specifically%20block%20growth%20at%20the%20microtubule%20%28-%29%20end.%20Structural%20data%20indicate%20that%20they%20do%20so%20by%20targeting%20the%20alpha-tubulin%20longitudinal%20surface.%20Interestingly%2C%20in%20one%20of%20the%20complexes%20studied%2C%20the%20alpha%20subunit%20is%20in%20a%20conformation%20that%20is%20intermediate%20between%20the%20ones%20most%20commonly%20observed%20in%20X-ray%20structures%20of%20tubulin%20and%20those%20seen%20in%20the%20microtubule%2C%20emphasizing%20the%20plasticity%20of%20tubulin.%20These%20alpha-tubulin-specific%20alpha%20Reps%20broaden%20the%20range%20of%20tools%20available%20for%20the%20mechanistic%20study%20of%20microtubule%20dynamics%20and%20its%20regulation.%22%2C%22date%22%3A%22MAR%205%202019%22%2C%22language%22%3A%22English%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.str.2018.12.001%22%2C%22ISSN%22%3A%220969-2126%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222020-03-11T13%3A31%3A49Z%22%7D%7D%2C%7B%22key%22%3A%22UYV2ALJW%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Naret%20et%20al.%22%2C%22parsedDate%22%3A%222019-02-28%22%2C%22numChildren%22%3A4%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ENaret%2C%20Timoth%26%23xE9%3Be%2C%20Ilhem%20Khelifi%2C%20Olivier%20Provot%2C%20J%26%23xE9%3Br%26%23xF4%3Bme%20Bignon%2C%20H%26%23xE9%3Bl%26%23xE8%3Bne%20Levaique%2C%20Joelle%20Dubois%2C%20Martin%20Souce%2C%20et%20al.%202019.%20%26%23x201C%3B1%2C1-Diheterocyclic%20Ethylenes%20Derived%20from%20Quinaldine%20and%20Carbazole%20as%20New%20Tubulin-Polymerization%20Inhibitors%3A%20Synthesis%2C%20Metabolism%2C%20and%20Biological%20Evaluation.%26%23x201D%3B%20%3Ci%3EJournal%20of%20Medicinal%20Chemistry%3C%5C%2Fi%3E%2062%20%284%29%3A%201902%26%23x2013%3B16.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1021%5C%2Facs.jmedchem.8b01386%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1021%5C%2Facs.jmedchem.8b01386%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%221%2C1-Diheterocyclic%20Ethylenes%20Derived%20from%20Quinaldine%20and%20Carbazole%20as%20New%20Tubulin-Polymerization%20Inhibitors%3A%20Synthesis%2C%20Metabolism%2C%20and%20Biological%20Evaluation%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Timoth%5Cu00e9e%22%2C%22lastName%22%3A%22Naret%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ilhem%22%2C%22lastName%22%3A%22Khelifi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Olivier%22%2C%22lastName%22%3A%22Provot%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22J%5Cu00e9r%5Cu00f4me%22%2C%22lastName%22%3A%22Bignon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22H%5Cu00e9l%5Cu00e8ne%22%2C%22lastName%22%3A%22Levaique%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Joelle%22%2C%22lastName%22%3A%22Dubois%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Martin%22%2C%22lastName%22%3A%22Souce%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Athena%22%2C%22lastName%22%3A%22Kasselouri%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alain%22%2C%22lastName%22%3A%22Deroussent%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ang%5Cu00e9lo%22%2C%22lastName%22%3A%22Paci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paloma%20F.%22%2C%22lastName%22%3A%22Varela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Mouad%22%2C%22lastName%22%3A%22Alami%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Abdallah%22%2C%22lastName%22%3A%22Hamze%22%7D%5D%2C%22abstractNote%22%3A%22We%20report%20the%20synthesis%20and%20metabolic%20and%20biological%20evaluation%20of%20a%20series%20of%2017%20novel%20heterocyclic%20derivatives%20of%20isocombretastatin-A4%20%28iso-CA-4%29%20and%20their%20structure-activity%20relationships.%20Among%20these%20derivatives%2C%20the%20most%20active%20compound%2C%204f%2C%20inhibited%20the%20growth%20of%20a%20panel%20of%20seven%20cancer%20cell%20lines%20with%20an%20IC50%20in%20the%20low%20nanomolar%20range.%20In%20addition%2C%204f%20showed%20interesting%20activity%20against%20CA-4-resistant%20colon-carcinoma%20cells%20and%20multidrug-resistant%20leukemia%20cells.%20It%20also%20induced%20G2%5C%2FM%20cell-cycle%20arrest.%20Structural%20data%20indicated%20binding%20of%204f%20to%20the%20colchicine%20site%20of%20tubulin%2C%20likely%20preventing%20the%20curved-to-straight%20tubulin%20structural%20changes%20that%20occur%20during%20microtubule%20assembly.%20Also%2C%204f%20disrupted%20the%20blood-vessel-like%20assembly%20formed%20by%20human%20umbilical-vein%20endothelial%20cells%20in%20vitro%2C%20suggesting%20its%20function%20as%20a%20vascular-disrupting%20agent.%20An%20in%20vitro%20metabolism%20study%20of%204f%20showed%20its%20high%20human-microsomal%20stability%20in%20comparison%20with%20that%20of%20iso-CA-4.%20The%20physicochemical%20properties%20of%204f%20may%20be%20conducive%20to%20CNS%20permeability%2C%20suggesting%20that%20this%20compound%20may%20be%20a%20possible%20candidate%20for%20the%20treatment%20of%20glioblastoma.%22%2C%22date%22%3A%22Feb%2028%2C%202019%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1021%5C%2Facs.jmedchem.8b01386%22%2C%22ISSN%22%3A%221520-4804%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222019-03-25T09%3A36%3A10Z%22%7D%7D%2C%7B%22key%22%3A%222YGCBQ7P%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Nguyen%20et%20al.%22%2C%22parsedDate%22%3A%222018-07-19%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ENguyen%2C%20T.%20Quyen%2C%20Magali%20Aumont-Ni%26%23xE7%3Baise%2C%20Jessica%20Andreani%2C%20Christophe%20Velours%2C%20M%26%23xE9%3Blanie%20Chenon%2C%20Fernando%20Vilela%2C%20Cl%26%23xE9%3Bmentine%20Geneste%2C%20Paloma%20Fern%26%23xE1%3Bndez%20Varela%2C%20Paola%20Llinas%2C%20and%20Julie%20M%26%23xE9%3Bn%26%23xE9%3Btrey.%202018.%20%26%23x201C%3BCharacterization%20of%20the%20Binding%20Mode%20of%20JNK-Interacting%20Protein%201%20%28JIP1%29%20to%20Kinesin-Light%20Chain%201%20%28KLC1%29.%26%23x201D%3B%20%3Ci%3EThe%20Journal%20of%20Biological%20Chemistry%3C%5C%2Fi%3E%20293%20%2836%29%3A%2013946%26%23x2013%3B60.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1074%5C%2Fjbc.RA118.003916%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1074%5C%2Fjbc.RA118.003916%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Characterization%20of%20the%20binding%20mode%20of%20JNK-interacting%20protein%201%20%28JIP1%29%20to%20kinesin-light%20chain%201%20%28KLC1%29%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22T.%20Quyen%22%2C%22lastName%22%3A%22Nguyen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Ni%5Cu00e7aise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jessica%22%2C%22lastName%22%3A%22Andreani%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%22%2C%22lastName%22%3A%22Velours%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M%5Cu00e9lanie%22%2C%22lastName%22%3A%22Chenon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Fernando%22%2C%22lastName%22%3A%22Vilela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cl%5Cu00e9mentine%22%2C%22lastName%22%3A%22Geneste%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paloma%20Fern%5Cu00e1ndez%22%2C%22lastName%22%3A%22Varela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paola%22%2C%22lastName%22%3A%22Llinas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Julie%22%2C%22lastName%22%3A%22M%5Cu00e9n%5Cu00e9trey%22%7D%5D%2C%22abstractNote%22%3A%22JIP1%20was%20first%20identified%20as%20scaffold%20protein%20for%20the%20MAP%20kinase%20JNK%20and%20is%20a%20cargo%20protein%20for%20the%20kinesin1%20molecular%20motor.%20JIP1%20plays%20significant%20and%20broad%20roles%20in%20neurons%2C%20mainly%20as%20a%20regulator%20of%20kinesin1-dependent%20transport%2C%20and%20is%20associated%20with%20human%20pathologies%20such%20as%20cancer%20and%20Alzheimer%20disease.%20JIP1%20is%20specifically%20recruited%20by%20the%20kinesin-light%20chain%201%20%28KLC1%29%20of%20kinesin1%2C%20but%20the%20details%20of%20this%20interaction%20are%20not%20yet%20fully%20elucidated.%20Here%2C%20using%20calorimetry%2C%20we%20extensively%20biochemically%20characterized%20the%20interaction%20between%20KLC1%20and%20JIP1.%20Using%20various%20truncated%20fragments%20of%20the%20tetratricopeptide%20repeat%20%28TPR%29%20domain%20of%20KLC1%2C%20we%20narrowed%20down%20its%20JIP1-binding%20region%20and%20identified%20seven%20KLC1%20residues%20critical%20for%20JIP1%20binding.%20These%20ITC-based%20binding%20data%20enabled%20us%20to%20footprint%20the%20JIP1-binding%20site%20on%20KLC1-TPR.%20This%20footprint%20was%20used%20to%20uncover%20the%20structural%20basis%20for%20the%20marginal%20inhibition%20of%20JIP1%20binding%20by%20the%20autoinhibitory%20LFP-acidic%20motif%20of%20KLC1%2C%20as%20well%20as%20for%20the%20competition%20between%20JIP1%20and%20another%20cargo%20protein%20of%20kinesin1%2C%20the%20W-acidic%20motif-containing%20Alcadein-%5Cu03b1.%20Also%2C%20we%20examined%20the%20role%20of%20each%20of%20these%20critical%20residues%20of%20KLC1%20for%20JIP1%20binding%20in%20the%20light%20of%20the%20previously%20reported%20crystal%20structure%20of%20the%20KLC1-TPR%3AJIP1%20complex.%20Finally%2C%20sequence%20search%20in%20eukaryotic%20genomes%20identified%20several%20proteins%2C%20among%20which%20SH2D6%20that%20exhibit%20similar%20motif%20to%20the%20KLC1-binding%20motif%20of%20JIP1.%20Overall%2C%20our%20extensive%20biochemical%20characterization%20of%20the%20KLC%3AJIP1%20interaction%2C%20as%20well%20as%20identification%20of%20potential%20KLC1-binding%20partners%20improve%20the%20understanding%20of%20how%20this%20growing%20family%20of%20cargos%20is%20recruited%20to%20kinesin1%20by%20KLC1.%22%2C%22date%22%3A%22Jul%2019%2C%202018%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1074%5C%2Fjbc.RA118.003916%22%2C%22ISSN%22%3A%221083-351X%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%2C%227EGDQ8LV%22%5D%2C%22dateModified%22%3A%222019-09-16T10%3A38%3A52Z%22%7D%7D%2C%7B%22key%22%3A%22TCN2Q4ET%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wang%20et%20al.%22%2C%22parsedDate%22%3A%222017-07-10%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWang%2C%20Weiyi%2C%20Soraya%20Cantos-Fernandes%2C%20Yuncong%20Lv%2C%20Hureshitanmu%20Kuerban%2C%20Shoeb%20Ahmad%2C%20Chunguang%20Wang%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202017.%20%26%23x201C%3BInsight%20into%20Microtubule%20Disassembly%20by%20Kinesin-13s%20from%20the%20Structure%20of%20Kif2C%20Bound%20to%20Tubulin.%26%23x201D%3B%20%3Ci%3ENature%20Communications%3C%5C%2Fi%3E%208%20%281%29%3A%2070.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41467-017-00091-9%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fs41467-017-00091-9%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Insight%20into%20microtubule%20disassembly%20by%20kinesin-13s%20from%20the%20structure%20of%20Kif2C%20bound%20to%20tubulin%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Weiyi%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Soraya%22%2C%22lastName%22%3A%22Cantos-Fernandes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuncong%22%2C%22lastName%22%3A%22Lv%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hureshitanmu%22%2C%22lastName%22%3A%22Kuerban%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Shoeb%22%2C%22lastName%22%3A%22Ahmad%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Chunguang%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22Kinesin-13s%20are%20critical%20microtubule%20regulators%20which%20induce%20microtubule%20disassembly%20in%20an%20ATP%20dependent%20manner.%20To%20clarify%20their%20mechanism%2C%20we%20report%20here%20the%20crystal%20structure%20of%20a%20functional%20construct%20of%20the%20kinesin-13%20Kif2C%5C%2FMCAK%20in%20an%20ATP-like%20state%20and%20bound%20to%20the%20%5Cu03b1%5Cu03b2-tubulin%20heterodimer%2C%20a%20complex%20mimicking%20the%20species%20that%20dissociates%20from%20microtubule%20ends%20during%20catalytic%20disassembly.%20Our%20results%20picture%20how%20Kif2C%20stabilizes%20a%20curved%20tubulin%20conformation.%20The%20Kif2C%20%5Cu03b14-L12-%5Cu03b15%20region%20undergoes%20a%20remarkable%2025%5Cu00b0%20rotation%20upon%20tubulin%20binding%20to%20target%20the%20%5Cu03b1%5Cu03b2-tubulin%20hinge.%20This%20movement%20leads%20the%20%5Cu03b25a-%5Cu03b25b%20motif%20to%20interact%20with%20the%20distal%20end%20of%20%5Cu03b2-tubulin%2C%20whereas%20the%20neck%20and%20the%20KVD%20motif%2C%20two%20specific%20elements%20of%20kinesin-13s%2C%20target%20the%20%5Cu03b1-tubulin%20distal%20end.%20Taken%20together%20with%20the%20study%20of%20Kif2C%20mutants%2C%20our%20data%20suggest%20that%20stabilization%20of%20a%20curved%20tubulin%20is%20an%20important%20contribution%20to%20the%20Kif2C%20mechanism.Kinesin-13s%20are%20microtubule%20depolymerizing%20enzymes.%20Here%20the%20authors%20present%20the%20crystal%20structure%20of%20a%20DARPin%20fused%20construct%20comprising%20the%20short%20neck%20region%20and%20motor%20domain%20of%20kinesin-13%20in%20complex%20with%20an%20%5Cu03b1%5Cu03b2-tubulin%20heterodimer%2C%20which%20shows%20that%20kinesin-13%20functions%20by%20stabilizing%20a%20curved%20tubulin%20conformation.%22%2C%22date%22%3A%22Jul%2010%2C%202017%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fs41467-017-00091-9%22%2C%22ISSN%22%3A%222041-1723%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T10%3A11%3A18Z%22%7D%7D%2C%7B%22key%22%3A%22ZXMRCDSC%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wang%20et%20al.%22%2C%22parsedDate%22%3A%222017-06-06%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWang%2C%20Yuxi%2C%20Yamei%20Yu%2C%20Guo-Bo%20Li%2C%20Shu-Ang%20Li%2C%20Chengyong%20Wu%2C%20Beno%26%23xEE%3Bt%20Gigant%2C%20Wenming%20Qin%2C%20et%20al.%202017.%20%26%23x201C%3BMechanism%20of%20Microtubule%20Stabilization%20by%20Taccalonolide%20AJ.%26%23x201D%3B%20%3Ci%3ENature%20Communications%3C%5C%2Fi%3E%208%20%28June%29%3A15787.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fncomms15787%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fncomms15787%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Mechanism%20of%20microtubule%20stabilization%20by%20taccalonolide%20AJ%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuxi%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yamei%22%2C%22lastName%22%3A%22Yu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Guo-Bo%22%2C%22lastName%22%3A%22Li%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Shu-Ang%22%2C%22lastName%22%3A%22Li%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Chengyong%22%2C%22lastName%22%3A%22Wu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Wenming%22%2C%22lastName%22%3A%22Qin%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hao%22%2C%22lastName%22%3A%22Chen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yangping%22%2C%22lastName%22%3A%22Wu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Qiang%22%2C%22lastName%22%3A%22Chen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jinliang%22%2C%22lastName%22%3A%22Yang%22%7D%5D%2C%22abstractNote%22%3A%22As%20a%20major%20component%20of%20the%20cytoskeleton%2C%20microtubules%20consist%20of%20%5Cu03b1%5Cu03b2-tubulin%20heterodimers%20and%20have%20been%20recognized%20as%20attractive%20targets%20for%20cancer%20chemotherapy.%20Microtubule-stabilizing%20agents%20%28MSAs%29%20promote%20polymerization%20of%20tubulin%20and%20stabilize%20the%20polymer%2C%20preventing%20depolymerization.%20The%20molecular%20mechanisms%20by%20which%20MSAs%20stabilize%20microtubules%20remain%20elusive.%20Here%20we%20report%20a%202.05%5Cu2009%5Cu00c5%20crystal%20structure%20of%20tubulin%20complexed%20with%20taccalonolide%20AJ%2C%20a%20newly%20identified%20taxane-site%20MSA.%20Taccalonolide%20AJ%20covalently%20binds%20to%20%5Cu03b2-tubulin%20D226.%20On%20AJ%20binding%2C%20the%20M-loop%20undergoes%20a%20conformational%20shift%20to%20facilitate%20tubulin%20polymerization.%20In%20this%20tubulin-AJ%20complex%2C%20the%20E-site%20of%20tubulin%20is%20occupied%20by%20GTP%20rather%20than%20GDP.%20Biochemical%20analyses%20confirm%20that%20AJ%20inhibits%20the%20hydrolysis%20of%20the%20E-site%20GTP.%20Thus%2C%20we%20propose%20that%20the%20%5Cu03b2-tubulin%20E-site%20is%20locked%20into%20a%20GTP-preferred%20status%20by%20AJ%20binding.%20Our%20results%20provide%20experimental%20evidence%20for%20the%20connection%20between%20MSA%20binding%20and%20tubulin%20nucleotide%20state%2C%20and%20will%20help%20design%20new%20MSAs%20to%20overcome%20taxane%20resistance.%22%2C%22date%22%3A%22Jun%2006%2C%202017%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1038%5C%2Fncomms15787%22%2C%22ISSN%22%3A%222041-1723%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T10%3A16%3A57Z%22%7D%7D%2C%7B%22key%22%3A%22AVKZVW7X%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Cao%20et%20al.%22%2C%22parsedDate%22%3A%222017-02-14%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ECao%2C%20Luyan%2C%20Soraya%20Cantos-Fernandes%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202017.%20%26%23x201C%3BThe%20Structural%20Switch%20of%20Nucleotide-Free%20Kinesin.%26%23x201D%3B%20%3Ci%3EScientific%20Reports%3C%5C%2Fi%3E%207%20%28February%29%3A42558.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fsrep42558%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fsrep42558%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22The%20structural%20switch%20of%20nucleotide-free%20kinesin%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Luyan%22%2C%22lastName%22%3A%22Cao%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Soraya%22%2C%22lastName%22%3A%22Cantos-Fernandes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222017-2-14%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1038%5C%2Fsrep42558%22%2C%22ISSN%22%3A%222045-2322%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fwww.nature.com%5C%2Farticles%5C%2Fsrep42558%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T11%3A46%3A41Z%22%7D%7D%2C%7B%22key%22%3A%2248XMY5ZZ%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Nguyen%20et%20al.%22%2C%22parsedDate%22%3A%222017%22%2C%22numChildren%22%3A4%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ENguyen%2C%20The%20Quyen%2C%20M%26%23xE9%3Blanie%20Chenon%2C%20Fernando%20Vilela%2C%20Christophe%20Velours%2C%20Magali%20Aumont-Nicaise%2C%20Jessica%20Andreani%2C%20Paloma%20F.%20Varela%2C%20Paola%20Llinas%2C%20and%20Julie%20M%26%23xE9%3Bn%26%23xE9%3Btrey.%202017.%20%26%23x201C%3BStructural%20Plasticity%20of%20the%20N-Terminal%20Capping%20Helix%20of%20the%20TPR%20Domain%20of%20Kinesin%20Light%20Chain.%26%23x201D%3B%20%3Ci%3EPloS%20One%3C%5C%2Fi%3E%2012%20%2810%29%3A%20e0186354.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1371%5C%2Fjournal.pone.0186354%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1371%5C%2Fjournal.pone.0186354%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structural%20plasticity%20of%20the%20N-terminal%20capping%20helix%20of%20the%20TPR%20domain%20of%20kinesin%20light%20chain%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22The%20Quyen%22%2C%22lastName%22%3A%22Nguyen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M%5Cu00e9lanie%22%2C%22lastName%22%3A%22Chenon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Fernando%22%2C%22lastName%22%3A%22Vilela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Christophe%22%2C%22lastName%22%3A%22Velours%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jessica%22%2C%22lastName%22%3A%22Andreani%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paloma%20F.%22%2C%22lastName%22%3A%22Varela%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paola%22%2C%22lastName%22%3A%22Llinas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Julie%22%2C%22lastName%22%3A%22M%5Cu00e9n%5Cu00e9trey%22%7D%5D%2C%22abstractNote%22%3A%22Kinesin1%20plays%20a%20major%20role%20in%20neuronal%20transport%20by%20recruiting%20many%20different%20cargos%20through%20its%20kinesin%20light%20chain%20%28KLC%29.%20Various%20structurally%20unrelated%20cargos%20interact%20with%20the%20conserved%20tetratricopeptide%20repeat%20%28TPR%29%20domain%20of%20KLC.%20The%20N-terminal%20capping%20helix%20of%20the%20TPR%20domain%20exhibits%20an%20atypical%20sequence%20and%20structural%20features%20that%20may%20contribute%20to%20the%20versatility%20of%20the%20TPR%20domain%20to%20bind%20different%20cargos.%20We%20determined%20crystal%20structures%20of%20the%20TPR%20domain%20of%20both%20KLC1%20and%20KLC2%20encompassing%20the%20N-terminal%20capping%20helix%20and%20show%20that%20this%20helix%20exhibits%20two%20distinct%20and%20defined%20orientations%20relative%20to%20the%20rest%20of%20the%20TPR%20domain.%20Such%20a%20difference%20in%20orientation%20gives%20rise%2C%20at%20the%20N-terminal%20part%20of%20the%20groove%2C%20to%20the%20formation%20of%20one%20hydrophobic%20pocket%2C%20as%20well%20as%20to%20electrostatic%20variations%20at%20the%20groove%20surface.%20We%20present%20a%20comprehensive%20structural%20analysis%20of%20available%20KLC1%5C%2F2-TPR%20domain%20structures%20that%20highlights%20that%20ligand%20binding%20into%20the%20groove%20can%20be%20specific%20of%20one%20or%20the%20other%20N-terminal%20capping%20helix%20orientations.%20Further%2C%20structural%20analysis%20reveals%20that%20the%20N-terminal%20capping%20helix%20is%20always%20involved%20in%20crystal%20packing%20contacts%2C%20especially%20in%20a%20TPR1%3ATPR1%27%20contact%20which%20highlights%20its%20propensity%20to%20be%20a%20protein-protein%20interaction%20site.%20Together%2C%20these%20results%20underline%20that%20the%20structural%20plasticity%20of%20the%20N-terminal%20capping%20helix%20might%20represent%20a%20structural%20determinant%20for%20TPR%20domain%20structural%20versatility%20in%20cargo%20binding.%22%2C%22date%22%3A%222017%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1371%5C%2Fjournal.pone.0186354%22%2C%22ISSN%22%3A%221932-6203%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T11%3A44%3A43Z%22%7D%7D%2C%7B%22key%22%3A%225RUPPRTM%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Ahmad%20et%20al.%22%2C%22parsedDate%22%3A%222016-07-06%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EAhmad%2C%20Shoeb%2C%20Ludovic%20Pecqueur%2C%20Birgit%20Dreier%2C%20Djemel%20Hamdane%2C%20Magali%20Aumont-Nicaise%2C%20Andreas%20Pl%26%23xFC%3Bckthun%2C%20Marcel%20Knossow%2C%20and%20Beno%26%23xEE%3Bt%20Gigant.%202016.%20%26%23x201C%3BDestabilizing%20an%20Interacting%20Motif%20Strengthens%20the%20Association%20of%20a%20Designed%20Ankyrin%20Repeat%20Protein%20with%20Tubulin.%26%23x201D%3B%20%3Ci%3EScientific%20Reports%3C%5C%2Fi%3E%206%20%28July%29%3A28922.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fsrep28922%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1038%5C%2Fsrep28922%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Destabilizing%20an%20interacting%20motif%20strengthens%20the%20association%20of%20a%20designed%20ankyrin%20repeat%20protein%20with%20tubulin%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Shoeb%22%2C%22lastName%22%3A%22Ahmad%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ludovic%22%2C%22lastName%22%3A%22Pecqueur%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Birgit%22%2C%22lastName%22%3A%22Dreier%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Djemel%22%2C%22lastName%22%3A%22Hamdane%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Andreas%22%2C%22lastName%22%3A%22Pl%5Cu00fcckthun%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marcel%22%2C%22lastName%22%3A%22Knossow%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222016-7-6%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1038%5C%2Fsrep28922%22%2C%22ISSN%22%3A%222045-2322%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fwww.nature.com%5C%2Farticles%5C%2Fsrep28922%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-15T12%3A41%3A13Z%22%7D%7D%2C%7B%22key%22%3A%22FETQWJAT%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Lippens%20et%20al.%22%2C%22parsedDate%22%3A%222016-06-07%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELippens%2C%20Guy%2C%20Isabelle%20Landrieu%2C%20Caroline%20Smet%2C%20Isabelle%20Huvent%2C%20Neha%20Gandhi%2C%20Beno%26%23xEE%3Bt%20Gigant%2C%20Cl%26%23xE9%3Bment%20Despres%2C%20Haoling%20Qi%2C%20and%20Juan%20Lopez.%202016.%20%26%23x201C%3BNMR%20Meets%20Tau%3A%20Insights%20into%20Its%20Function%20and%20Pathology.%26%23x201D%3B%20%3Ci%3EBiomolecules%3C%5C%2Fi%3E%206%20%282%29%3A%2028.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3390%5C%2Fbiom6020028%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.3390%5C%2Fbiom6020028%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22NMR%20Meets%20Tau%3A%20Insights%20into%20Its%20Function%20and%20Pathology%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Guy%22%2C%22lastName%22%3A%22Lippens%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Isabelle%22%2C%22lastName%22%3A%22Landrieu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Caroline%22%2C%22lastName%22%3A%22Smet%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Isabelle%22%2C%22lastName%22%3A%22Huvent%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Neha%22%2C%22lastName%22%3A%22Gandhi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Cl%5Cu00e9ment%22%2C%22lastName%22%3A%22Despres%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Haoling%22%2C%22lastName%22%3A%22Qi%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Juan%22%2C%22lastName%22%3A%22Lopez%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222016-06-07%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.3390%5C%2Fbiom6020028%22%2C%22ISSN%22%3A%222218-273X%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fwww.mdpi.com%5C%2F2218-273X%5C%2F6%5C%2F2%5C%2F28%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T11%3A34%3A01Z%22%7D%7D%2C%7B%22key%22%3A%22AAQ5CTJ8%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Llinas%20et%20al.%22%2C%22parsedDate%22%3A%222016-03-01%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3ELlinas%2C%20Paola%2C%20M%26%23xE9%3Blanie%20Chenon%2C%20T.%20Quyen%20Nguyen%2C%20Catia%20Moreira%2C%20Ann%26%23xE9%3Blie%20de%20R%26%23xE9%3Bgibus%2C%20Aline%20Coquard%2C%20Maria%20J.%20Ramos%2C%20Rapha%26%23xEB%3Bl%20Gu%26%23xE9%3Brois%2C%20Pedro%20A.%20Fernandes%2C%20and%20Julie%20M%26%23xE9%3Bn%26%23xE9%3Btrey.%202016.%20%26%23x201C%3BStructure%20of%20a%20Truncated%20Form%20of%20Leucine%20Zipper%20II%20of%20JIP3%20Reveals%20an%20Unexpected%20Antiparallel%20Coiled-Coil%20Arrangement.%26%23x201D%3B%20%3Ci%3EActa%20Crystallographica%20Section%20F%20Structural%20Biology%20Communications%3C%5C%2Fi%3E%2072%20%283%29%3A%20198%26%23x2013%3B206.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1107%5C%2FS2053230X16001576%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1107%5C%2FS2053230X16001576%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structure%20of%20a%20truncated%20form%20of%20leucine%20zipper%20II%20of%20JIP3%20reveals%20an%20unexpected%20antiparallel%20coiled-coil%20arrangement%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Paola%22%2C%22lastName%22%3A%22Llinas%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22M%5Cu00e9lanie%22%2C%22lastName%22%3A%22Chenon%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22T.%20Quyen%22%2C%22lastName%22%3A%22Nguyen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Catia%22%2C%22lastName%22%3A%22Moreira%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ann%5Cu00e9lie%22%2C%22lastName%22%3A%22de%20R%5Cu00e9gibus%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Aline%22%2C%22lastName%22%3A%22Coquard%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Maria%20J.%22%2C%22lastName%22%3A%22Ramos%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Rapha%5Cu00ebl%22%2C%22lastName%22%3A%22Gu%5Cu00e9rois%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Pedro%20A.%22%2C%22lastName%22%3A%22Fernandes%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Julie%22%2C%22lastName%22%3A%22M%5Cu00e9n%5Cu00e9trey%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222016-03-01%22%2C%22language%22%3A%22%22%2C%22DOI%22%3A%2210.1107%5C%2FS2053230X16001576%22%2C%22ISSN%22%3A%222053-230X%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fscripts.iucr.org%5C%2Fcgi-bin%5C%2Fpaper%3FS2053230X16001576%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T11%3A43%3A14Z%22%7D%7D%2C%7B%22key%22%3A%22ZMSDSIQS%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Fetics%20et%20al.%22%2C%22parsedDate%22%3A%222016-02-02%22%2C%22numChildren%22%3A2%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EFetics%2C%20Susan%2C%20Aur%26%23xE9%3Blien%20Thureau%2C%20Val%26%23xE9%3Brie%20Campanacci%2C%20Magali%20Aumont-Nicaise%2C%20Ir%26%23xE8%3Bne%20Dang%2C%20Alexis%20Gautreau%2C%20Javier%20P%26%23xE9%3Brez%2C%20and%20Jacqueline%20Cherfils.%202016.%20%26%23x201C%3BHybrid%20Structural%20Analysis%20of%20the%20Arp2%5C%2F3%20Regulator%20Arpin%20Identifies%20Its%20Acidic%20Tail%20as%20a%20Primary%20Binding%20Epitope.%26%23x201D%3B%20%3Ci%3EStructure%20%28London%2C%20England%3A%201993%29%3C%5C%2Fi%3E%2024%20%282%29%3A%20252%26%23x2013%3B60.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.str.2015.12.001%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1016%5C%2Fj.str.2015.12.001%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Hybrid%20Structural%20Analysis%20of%20the%20Arp2%5C%2F3%20Regulator%20Arpin%20Identifies%20Its%20Acidic%20Tail%20as%20a%20Primary%20Binding%20Epitope%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Susan%22%2C%22lastName%22%3A%22Fetics%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Aur%5Cu00e9lien%22%2C%22lastName%22%3A%22Thureau%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Val%5Cu00e9rie%22%2C%22lastName%22%3A%22Campanacci%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Magali%22%2C%22lastName%22%3A%22Aumont-Nicaise%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ir%5Cu00e8ne%22%2C%22lastName%22%3A%22Dang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Alexis%22%2C%22lastName%22%3A%22Gautreau%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Javier%22%2C%22lastName%22%3A%22P%5Cu00e9rez%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jacqueline%22%2C%22lastName%22%3A%22Cherfils%22%7D%5D%2C%22abstractNote%22%3A%22Arpin%20is%20a%20newly%20discovered%20regulator%20of%20actin%20polymerization%20at%20the%20cell%20leading%20edge%2C%20which%20steers%20cell%20migration%20by%20exerting%20a%20negative%20control%20on%20the%20Arp2%5C%2F3%20complex.%20Arpin%20proteins%20have%20an%20acidic%20tail%20homologous%20to%20the%20acidic%20motif%20of%20the%20VCA%20domain%20of%20nucleation-promoting%20factors%20%28NPFs%29.%20This%20tail%20is%20predicted%20to%20compete%20with%20the%20VCA%20of%20NPFs%20for%20binding%20to%20the%20Arp2%5C%2F3%20complex%2C%20thereby%20mitigating%20activation%20and%5C%2For%20tethering%20of%20the%20complex%20to%20sites%20of%20actin%20branching.%20Here%2C%20we%20investigated%20the%20structure%20of%20full-length%20Arpin%20using%20synchrotron%20small-angle%20X-ray%20scattering%2C%20and%20of%20its%20acidic%20tail%20in%20complex%20with%20an%20ankyrin%20repeats%20domain%20using%20X-ray%20crystallography.%20The%20data%20were%20combined%20in%20a%20hybrid%20model%20in%20which%20the%20acidic%20tail%20extends%20from%20the%20globular%20core%20as%20a%20linear%20peptide%20and%20forms%20a%20primary%20epitope%20that%20is%20readily%20accessible%20in%20unbound%20Arpin%20and%20suffices%20to%20tether%20Arpin%20to%20interacting%20proteins%20with%20high%20affinity.%22%2C%22date%22%3A%22Feb%2002%2C%202016%22%2C%22language%22%3A%22eng%22%2C%22DOI%22%3A%2210.1016%5C%2Fj.str.2015.12.001%22%2C%22ISSN%22%3A%221878-4186%22%2C%22url%22%3A%22%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T10%3A10%3A13Z%22%7D%7D%2C%7B%22key%22%3A%22I8AJQ65I%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wang%20et%20al.%22%2C%22parsedDate%22%3A%222016%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWang%2C%20Yuxi%2C%20Hang%20Zhang%2C%20Beno%26%23xEE%3Bt%20Gigant%2C%20Yamei%20Yu%2C%20Yangping%20Wu%2C%20Xiangzheng%20Chen%2C%20Qinhuai%20Lai%2C%20Zhaoya%20Yang%2C%20Qiang%20Chen%2C%20and%20Jinliang%20Yang.%202016.%20%26%23x201C%3BStructures%20of%20a%20Diverse%20Set%20of%20Colchicine%20Binding%20Site%20Inhibitors%20in%20Complex%20with%20Tubulin%20Provide%20a%20Rationale%20for%20Drug%20Discovery.%26%23x201D%3B%20%3Ci%3EFEBS%20Journal%3C%5C%2Fi%3E%20283%20%281%29%3A%20102%26%23x2013%3B11.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1111%5C%2Ffebs.13555%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1111%5C%2Ffebs.13555%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Structures%20of%20a%20diverse%20set%20of%20colchicine%20binding%20site%20inhibitors%20in%20complex%20with%20tubulin%20provide%20a%20rationale%20for%20drug%20discovery%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuxi%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hang%22%2C%22lastName%22%3A%22Zhang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yamei%22%2C%22lastName%22%3A%22Yu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yangping%22%2C%22lastName%22%3A%22Wu%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Xiangzheng%22%2C%22lastName%22%3A%22Chen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Qinhuai%22%2C%22lastName%22%3A%22Lai%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Zhaoya%22%2C%22lastName%22%3A%22Yang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Qiang%22%2C%22lastName%22%3A%22Chen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Jinliang%22%2C%22lastName%22%3A%22Yang%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%2201%5C%2F2016%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.1111%5C%2Ffebs.13555%22%2C%22ISSN%22%3A%221742464X%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fdoi.wiley.com%5C%2F10.1111%5C%2Ffebs.13555%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222018-03-22T11%3A43%3A28Z%22%7D%7D%2C%7B%22key%22%3A%22HKCJXXZW%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wang%20et%20al.%22%2C%22parsedDate%22%3A%222015%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWang%2C%20Weiyi%2C%20Ting%20Shen%2C%20Raphael%20Guerois%2C%20Fuming%20Zhang%2C%20Hureshitanmu%20Kuerban%2C%20Yuncong%20Lv%2C%20Beno%26%23xEE%3Bt%20Gigant%2C%20Marcel%20Knossow%2C%20and%20Chunguang%20Wang.%202015.%20%26%23x201C%3BNew%20Insights%20into%20the%20Coupling%20between%20Microtubule%20Depolymerization%20and%20ATP%20Hydrolysis%20by%20Kinesin-13%20Protein%20Kif2C.%26%23x201D%3B%20%3Ci%3EJournal%20of%20Biological%20Chemistry%3C%5C%2Fi%3E%20290%20%2830%29%3A%2018721%26%23x2013%3B31.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1074%5C%2Fjbc.M115.646919%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1074%5C%2Fjbc.M115.646919%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22New%20Insights%20into%20the%20Coupling%20between%20Microtubule%20Depolymerization%20and%20ATP%20Hydrolysis%20by%20Kinesin-13%20Protein%20Kif2C%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Weiyi%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Ting%22%2C%22lastName%22%3A%22Shen%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Raphael%22%2C%22lastName%22%3A%22Guerois%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Fuming%22%2C%22lastName%22%3A%22Zhang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Hureshitanmu%22%2C%22lastName%22%3A%22Kuerban%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Yuncong%22%2C%22lastName%22%3A%22Lv%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marcel%22%2C%22lastName%22%3A%22Knossow%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Chunguang%22%2C%22lastName%22%3A%22Wang%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222015%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.1074%5C%2Fjbc.M115.646919%22%2C%22ISSN%22%3A%220021-9258%2C%201083-351X%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fwww.jbc.org%5C%2Flookup%5C%2Fdoi%5C%2F10.1074%5C%2Fjbc.M115.646919%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222021-03-16T15%3A57%3A03Z%22%7D%7D%2C%7B%22key%22%3A%229N568G35%22%2C%22library%22%3A%7B%22id%22%3A3888256%7D%2C%22meta%22%3A%7B%22creatorSummary%22%3A%22Wang%20et%20al.%22%2C%22parsedDate%22%3A%222015%22%2C%22numChildren%22%3A0%7D%2C%22bib%22%3A%22%3Cdiv%20class%3D%5C%22csl-bib-body%5C%22%20style%3D%5C%22line-height%3A%201.35%3B%20padding-left%3A%201em%3B%20text-indent%3A-1em%3B%5C%22%3E%5Cn%20%20%3Cdiv%20class%3D%5C%22csl-entry%5C%22%3EWang%2C%20Weiyi%2C%20Luyan%20Cao%2C%20Chunguang%20Wang%2C%20Beno%26%23xEE%3Bt%20Gigant%2C%20and%20Marcel%20Knossow.%202015.%20%26%23x201C%3BKinesin%2C%2030%20Years%20Later%3A%20Recent%20Insights%20from%20Structural%20Studies%3A%20Kinesin%2C%2030%20Years%20Later%3A%20Structural%20Insights.%26%23x201D%3B%20%3Ci%3EProtein%20Science%3C%5C%2Fi%3E%2024%20%287%29%3A%201047%26%23x2013%3B56.%20%3Ca%20class%3D%27zp-DOIURL%27%20href%3D%27https%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1002%5C%2Fpro.2697%27%3Ehttps%3A%5C%2F%5C%2Fdoi.org%5C%2F10.1002%5C%2Fpro.2697%3C%5C%2Fa%3E.%3C%5C%2Fdiv%3E%5Cn%3C%5C%2Fdiv%3E%22%2C%22data%22%3A%7B%22itemType%22%3A%22journalArticle%22%2C%22title%22%3A%22Kinesin%2C%2030%20years%20later%3A%20Recent%20insights%20from%20structural%20studies%3A%20Kinesin%2C%2030%20Years%20Later%3A%20Structural%20Insights%22%2C%22creators%22%3A%5B%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Weiyi%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Luyan%22%2C%22lastName%22%3A%22Cao%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Chunguang%22%2C%22lastName%22%3A%22Wang%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Beno%5Cu00eet%22%2C%22lastName%22%3A%22Gigant%22%7D%2C%7B%22creatorType%22%3A%22author%22%2C%22firstName%22%3A%22Marcel%22%2C%22lastName%22%3A%22Knossow%22%7D%5D%2C%22abstractNote%22%3A%22%22%2C%22date%22%3A%222015%22%2C%22language%22%3A%22en%22%2C%22DOI%22%3A%2210.1002%5C%2Fpro.2697%22%2C%22ISSN%22%3A%2209618368%22%2C%22url%22%3A%22http%3A%5C%2F%5C%2Fdoi.wiley.com%5C%2F10.1002%5C%2Fpro.2697%22%2C%22collections%22%3A%5B%22R7I3GKDL%22%5D%2C%22dateModified%22%3A%222021-03-16T15%3A57%3A11Z%22%7D%7D%5D%7D
Ammar Khodja, Liza, Valérie Campanacci, Guy Lippens, and Benoît Gigant. 2024. “The Structure of a Tau Fragment Bound to Tubulin Prompts New Hypotheses on Tau Mechanism and Oligomerization.” PNAS Nexus 3 (11): pgae487. https://doi.org/10.1093/pnasnexus/pgae487.
Van Blerkom, Peter, Armel Bezault, Cécile Sauvanet, Dorit Hanein, and Niels Volkmann. 2024. “The GoldX Fiducial Eraser.” International Journal of Molecular Sciences 25 (13): 7442. https://doi.org/10.3390/ijms25137442.
Campanacci, Valérie, and Benoît Gigant. 2023. “The C-Terminus of Stathmin-like Proteins Governs the Stability of Their Complexes with Tubulin.” Biochemical and Biophysical Research Communications 682 (October):244–49. https://doi.org/10.1016/j.bbrc.2023.10.023.
Teixeira-Nunes, Magda, Pascal Retailleau, Dorothée Raoux-Barbot, Martine Comisso, Anani Amegan Missinou, Christophe Velours, Stéphane Plancqueel, Daniel Ladant, Undine Mechold, and Louis Renault. 2023. “Functional and Structural Insights into the Multi-Step Activation and Catalytic Mechanism of Bacterial ExoY Nucleotidyl Cyclase Toxins Bound to Actin-Profilin.” PLoS Pathogens 19 (9): e1011654. https://doi.org/10.1371/journal.ppat.1011654.
Teixeira-Nunes, Magda, Pascal Retailleau, Martine Comisso, Vincent Deruelle, Undine Mechold, and Louis Renault. 2022. “Bacterial Nucleotidyl Cyclases Activated by Calmodulin or Actin in Host Cells: Enzyme Specificities and Cytotoxicity Mechanisms Identified to Date.” International Journal of Molecular Sciences 23 (12): 6743. https://doi.org/10.3390/ijms23126743.
Campanacci, Valérie, Agathe Urvoas, Liza Ammar Khodja, Magali Aumont-Nicaise, Magali Noiray, Sylvie Lachkar, Patrick A. Curmi, Philippe Minard, and Benoît Gigant. 2022. “Structural Convergence for Tubulin Binding of CPAP and Vinca Domain Microtubule Inhibitors.” Proceedings of the National Academy of Sciences 119 (19): e2120098119. https://doi.org/10.1073/pnas.2120098119.
Stein, Andreas, Persefoni Hilken née Thomopoulou, Corazon Frias, Sina M. Hopff, Paloma Varela, Nicola Wilke, Arul Mariappan, et al. 2022. “B-nor-Methylene Colchicinoid PT-100 Selectively Induces Apoptosis in Multidrug-Resistant Human Cancer Cells via an Intrinsic Pathway in a Caspase-Independent Manner.” ACS Omega 7 (3): 2591–2603. https://doi.org/10.1021/acsomega.1c04659.
Seul, Anait, Sandrine Brasilès, Isabelle Petitpas, Rudi Lurz, Valérie Campanacci, Christian Cambillau, Frank Weise, Mohamed Zairi, Paulo Tavares, and Isabelle Auzat. 2021. “Biogenesis of a Bacteriophage Long Non-Contractile Tail.” Journal of Molecular Biology 433 (18): 167112. https://doi.org/10.1016/j.jmb.2021.167112.
Ayukawa, Rie, Seigo Iwata, Hiroshi Imai, Shinji Kamimura, Masahito Hayashi, Kien Xuan Ngo, Itsushi Minoura, et al. 2021. “GTP-Dependent Formation of Straight Tubulin Oligomers Leads to Microtubule Nucleation.” Journal of Cell Biology 220 (e202007033). https://doi.org/10.1083/jcb.202007033.
Varela, Paloma F., Mélanie Chenon, Christophe Velours, Kristen J. Verhey, Julie Ménétrey, and Benoît Gigant. 2021. “Structural Snapshots of the Kinesin-2 OSM-3 along Its Nucleotide Cycle: Implications for the ATP Hydrolysis Mechanism.” FEBS Open Bio 11 (3): 564–77. https://doi.org/10.1002/2211-5463.13101.
Silistre, Hazel, Dorothée Raoux-Barbot, Federica Mancinelli, Flora Sangouard, Alice Dupin, Alexander Belyy, Vincent Deruelle, et al. 2021. “Prevalence of ExoY Activity in Pseudomonas Aeruginosa Reference Panel Strains and Impact on Cytotoxicity in Epithelial Cells.” Frontiers in Microbiology 12:666097. https://doi.org/10.3389/fmicb.2021.666097.
Shchegravina, Ekaterina S., Elena V. Svirshchevskaya, Sebastien Combes, Diane Allegro, Pascale Barbier, Benoit Gigant, Paloma F. Varela, et al. 2020. “Discovery of Dihydrofuranoallocolchicinoids - Highly Potent Antimitotic Agents with Low Acute Toxicity.” European Journal of Medicinal Chemistry 207 (December):112724. https://doi.org/10.1016/j.ejmech.2020.112724.
Knossow, Marcel, Valérie Campanacci, Liza Ammar Khodja, and Benoît Gigant. 2020. “The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies.” IScience 23 (9): 101511. https://doi.org/10.1016/j.isci.2020.101511.
Vilela, Fernando, Christophe Velours, Mélanie Chenon, Magali Aumont-Nicaise, Valérie Campanacci, Aurélien Thureau, Olena Pylypenko, Jessica Andreani, Paola Llinas, and Julie Ménétrey. 2019. “Structural Characterization of the RH1-LZI Tandem of JIP3/4 Highlights RH1 Domains as a Cytoskeletal Motor-Binding Motif.” Scientific Reports 9 (1): 16036. https://doi.org/10.1038/s41598-019-52537-3.
Lippens, Guy, and Benoît Gigant. 2019. “Elucidating Tau Function and Dysfunction in the Era of Cryo-EM.” The Journal of Biological Chemistry 294 (24): 9316–25. https://doi.org/10.1074/jbc.REV119.008031.
Campanacci, Valérie, Agathe Urvoas, Soraya Cantos-Fernandes, Magali Aumont-Nicaise, Ana-Andreea Arteni, Christophe Velours, Marie Valerio-Lepiniec, et al. 2019. “Insight into Microtubule Nucleation from Tubulin-Capping Proteins.” Proceedings of the National Academy of Sciences of the United States of America 116 (20): 9859–64. https://doi.org/10.1073/pnas.1813559116.
Campanacci, Valerie, Agathe Urvoas, Tanja Consolati, Soraya Cantos-Fernandes, Magali Aumont-Nicaise, Marie Valerio-Lepiniec, Thomas Surrey, Philippe Minard, and Benoit Gigant. 2019. “Selection and Characterization of Artificial Proteins Targeting the Tubulin Alpha Subunit.” Structure 27 (3): 497–506. https://doi.org/10.1016/j.str.2018.12.001.
Naret, Timothée, Ilhem Khelifi, Olivier Provot, Jérôme Bignon, Hélène Levaique, Joelle Dubois, Martin Souce, et al. 2019. “1,1-Diheterocyclic Ethylenes Derived from Quinaldine and Carbazole as New Tubulin-Polymerization Inhibitors: Synthesis, Metabolism, and Biological Evaluation.” Journal of Medicinal Chemistry 62 (4): 1902–16. https://doi.org/10.1021/acs.jmedchem.8b01386.
Nguyen, T. Quyen, Magali Aumont-Niçaise, Jessica Andreani, Christophe Velours, Mélanie Chenon, Fernando Vilela, Clémentine Geneste, Paloma Fernández Varela, Paola Llinas, and Julie Ménétrey. 2018. “Characterization of the Binding Mode of JNK-Interacting Protein 1 (JIP1) to Kinesin-Light Chain 1 (KLC1).” The Journal of Biological Chemistry 293 (36): 13946–60. https://doi.org/10.1074/jbc.RA118.003916.
Wang, Weiyi, Soraya Cantos-Fernandes, Yuncong Lv, Hureshitanmu Kuerban, Shoeb Ahmad, Chunguang Wang, and Benoît Gigant. 2017. “Insight into Microtubule Disassembly by Kinesin-13s from the Structure of Kif2C Bound to Tubulin.” Nature Communications 8 (1): 70. https://doi.org/10.1038/s41467-017-00091-9.
Wang, Yuxi, Yamei Yu, Guo-Bo Li, Shu-Ang Li, Chengyong Wu, Benoît Gigant, Wenming Qin, et al. 2017. “Mechanism of Microtubule Stabilization by Taccalonolide AJ.” Nature Communications 8 (June):15787. https://doi.org/10.1038/ncomms15787.
Cao, Luyan, Soraya Cantos-Fernandes, and Benoît Gigant. 2017. “The Structural Switch of Nucleotide-Free Kinesin.” Scientific Reports 7 (February):42558. https://doi.org/10.1038/srep42558.
Nguyen, The Quyen, Mélanie Chenon, Fernando Vilela, Christophe Velours, Magali Aumont-Nicaise, Jessica Andreani, Paloma F. Varela, Paola Llinas, and Julie Ménétrey. 2017. “Structural Plasticity of the N-Terminal Capping Helix of the TPR Domain of Kinesin Light Chain.” PloS One 12 (10): e0186354. https://doi.org/10.1371/journal.pone.0186354.
Ahmad, Shoeb, Ludovic Pecqueur, Birgit Dreier, Djemel Hamdane, Magali Aumont-Nicaise, Andreas Plückthun, Marcel Knossow, and Benoît Gigant. 2016. “Destabilizing an Interacting Motif Strengthens the Association of a Designed Ankyrin Repeat Protein with Tubulin.” Scientific Reports 6 (July):28922. https://doi.org/10.1038/srep28922.
Lippens, Guy, Isabelle Landrieu, Caroline Smet, Isabelle Huvent, Neha Gandhi, Benoît Gigant, Clément Despres, Haoling Qi, and Juan Lopez. 2016. “NMR Meets Tau: Insights into Its Function and Pathology.” Biomolecules 6 (2): 28. https://doi.org/10.3390/biom6020028.
Llinas, Paola, Mélanie Chenon, T. Quyen Nguyen, Catia Moreira, Annélie de Régibus, Aline Coquard, Maria J. Ramos, Raphaël Guérois, Pedro A. Fernandes, and Julie Ménétrey. 2016. “Structure of a Truncated Form of Leucine Zipper II of JIP3 Reveals an Unexpected Antiparallel Coiled-Coil Arrangement.” Acta Crystallographica Section F Structural Biology Communications 72 (3): 198–206. https://doi.org/10.1107/S2053230X16001576.
Fetics, Susan, Aurélien Thureau, Valérie Campanacci, Magali Aumont-Nicaise, Irène Dang, Alexis Gautreau, Javier Pérez, and Jacqueline Cherfils. 2016. “Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.” Structure (London, England: 1993) 24 (2): 252–60. https://doi.org/10.1016/j.str.2015.12.001.
Wang, Yuxi, Hang Zhang, Benoît Gigant, Yamei Yu, Yangping Wu, Xiangzheng Chen, Qinhuai Lai, Zhaoya Yang, Qiang Chen, and Jinliang Yang. 2016. “Structures of a Diverse Set of Colchicine Binding Site Inhibitors in Complex with Tubulin Provide a Rationale for Drug Discovery.” FEBS Journal 283 (1): 102–11. https://doi.org/10.1111/febs.13555.
Wang, Weiyi, Ting Shen, Raphael Guerois, Fuming Zhang, Hureshitanmu Kuerban, Yuncong Lv, Benoît Gigant, Marcel Knossow, and Chunguang Wang. 2015. “New Insights into the Coupling between Microtubule Depolymerization and ATP Hydrolysis by Kinesin-13 Protein Kif2C.” Journal of Biological Chemistry 290 (30): 18721–31. https://doi.org/10.1074/jbc.M115.646919.
Wang, Weiyi, Luyan Cao, Chunguang Wang, Benoît Gigant, and Marcel Knossow. 2015. “Kinesin, 30 Years Later: Recent Insights from Structural Studies: Kinesin, 30 Years Later: Structural Insights.” Protein Science 24 (7): 1047–56. https://doi.org/10.1002/pro.2697.