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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Christophe LE CLAINCHE & Louis RENAULT : Dynamique du cytosquelette et motilité

pubmed : ( ( (( "le clainche ...

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NCBI : db=pubmed ; Term=( ( (( "Le clainche C"[author] OR "Renault L"[author] OR "DAVID V"[author] OR "LAI TL"[author] OR "HENRIOT V"[author] OR ("WANG H"[author] AND "Le clainche C"[author]) OR ("FELLOUS S"[author] AND "RENAULT L"[author]) ) AND "2014/01/01"[Date - Publication] : "3000"[Date - Publication] ) OR ( "2014/01/01"[Date - Publication] : "2018/01/01"[Date - Publication] AND ("Carlier MF"[author] OR (("Ciobanasu C"[author] OR "Faivre B"[author]) AND "Le clainche C"[author]) OR (("PERNIER J"[author] OR "MONTAVILLE P"[author] OR "Shekhar S"[author] OR "Kühn S"[author] OR "Guichard B"[author] OR "Jiao Y"[author] OR "COMPPER C"[author]) AND "Carlier MF"[author]) ) ) ) AND ("Laboratoire d’Enzymologie et Biochimie Structurales"[Affiliation] OR I2BC[Affiliation] OR "Institute for Integrative Biology of the Cell"[Affiliation] ) OR ("LAI TL"[author] AND "2016/01/01"[Date - Publication] : "3000"[Date - Publication] AND "iBiTec-s"[Affiliation]) )

Articles syndiqués

  • The trimeric coiled-coil HSBP1 protein promotes WASH complex assembly at centrosomes.

    1er juin, par Visweshwaran SP, Thomason PA, Guerois R, Vacher S, Denisov EV, Tashireva LA, Lomakina ME, Lazennec-Schurdevin C, Lakisic G, Lilla S, Molinie N, Henriot V, Mechulam Y, Alexandrova AY, Cherdyntseva NV, Bièche I, Schmitt E, Insall RH, Gautreau A
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    The trimeric coiled-coil HSBP1 protein promotes WASH complex assembly at centrosomes.

    EMBO J. 2018 May 29;:

    Authors: Visweshwaran SP, Thomason PA, Guerois R, Vacher S, Denisov EV, Tashireva LA, Lomakina ME, Lazennec-Schurdevin C, Lakisic G, Lilla S, Molinie N, Henriot V, Mechulam Y, Alexandrova AY, Cherdyntseva NV, Bièche I, Schmitt E, Insall RH, Gautreau A

    Abstract
    The Arp2/3 complex generates branched actin networks that exert pushing forces onto different cellular membranes. WASH complexes activate Arp2/3 complexes at the surface of endosomes and thereby fission transport intermediates containing endocytosed receptors, such as α5β1 integrins. How WASH complexes are assembled in the cell is unknown. Here, we identify the small coiled-coil protein HSBP1 as a factor that specifically promotes the assembly of a ternary complex composed of CCDC53, WASH, and FAM21 by dissociating the CCDC53 homotrimeric precursor. HSBP1 operates at the centrosome, which concentrates the building blocks. HSBP1 depletion in human cancer cell lines and in Dictyostelium amoebae phenocopies WASH depletion, suggesting a critical role of the ternary WASH complex for WASH functions. HSBP1 is required for the development of focal adhesions and of cell polarity. These defects impair the migration and invasion of tumor cells. Overexpression of HSBP1 in breast tumors is associated with increased levels of WASH complexes and with poor prognosis for patients.

    PMID: 29844016 [PubMed - as supplied by publisher]

  • Integrin-bound talin head inhibits actin filament barbed end elongation.

    26 décembre 2017, par Ciobanasu C, Wang H, Henriot V, Mathieu C, Fente A, Csillag S, Vigouroux C, Faivre B, Le Clainche C
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    Integrin-bound talin head inhibits actin filament barbed end elongation.

    J Biol Chem. 2017 Dec 24;:

    Authors: Ciobanasu C, Wang H, Henriot V, Mathieu C, Fente A, Csillag S, Vigouroux C, Faivre B, Le Clainche C

    Abstract
    Focal adhesions (FAs) mechanically couple the extracellular matrix (ECM) to the dynamic actin cytoskeleton, via transmembrane integrins and actin-binding proteins. The molecular mechanisms by which protein machineries control force transmission along this molecular axis, i.e. modulating integrin activation and controlling actin polymerization, remain largely unknown. Talin is a major actin-binding protein that controls both the inside-out activation of integrins and actin-filament anchoring and thus plays a major role in the establishment of the actin-ECM mechanical coupling. Talin contains three actin-binding domains (ABDs). The N-terminal head domain contains both the F3 integrin-activating domain and ABD1, while the C-terminal rod contains the actin-anchoring ABD2 and ABD3. Integrin binding is regulated by an intramolecular interaction between the N-terminal head and a C-terminal five-helix-bundle (R9). Whether talin ABDs regulate actin polymerization in a constitutive or regulated manner has not been fully explored. Here, we combine kinetics assays using fluorescence spectroscopy and single actin filament observation in TIRF microscopy, to examine relevant functions of the three ABDs of talin. We find that the N-terminal ABD1 blocks actin filament barbed end elongation while ABD2 and ABD3 do not show any activity. By mutating residues in ABD1, we find that this activity is mediated by a positively charged surface that is partially masked by its intramolecular interaction with R9. Our results also demonstrate that, once this intramolecular interaction is released, integrin-bound talin head retains the ability to inhibit actin assembly.

    PMID: 29276177 [PubMed - as supplied by publisher]

  • ExoY, an actin-activated nucleotidyl cyclase toxin from P. aeruginosa : A minireview.

    21 décembre 2017, par Belyy A, Mechold U, Renault L, Ladant D
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    ExoY, an actin-activated nucleotidyl cyclase toxin from P. aeruginosa: A minireview.

    Toxicon. 2017 Dec 16;:

    Authors: Belyy A, Mechold U, Renault L, Ladant D

    Abstract
    ExoY is one of four well-characterized Pseudomonas aeruginosa type 3 secretion system (T3SS) effectors. It is a nucleotidyl cyclase toxin that is inactive inside the bacteria, but becomes potently activated once it is delivered into the eukaryotic target cells. Recently, filamentous actin was identified as the eukaryotic cofactor that stimulates specifically ExoY enzymatic activity by several orders of magnitude. In this review, we discuss recent advances in understanding the biochemistry of nucleotidyl cyclase activity of ExoY and its regulation by interaction with filamentous actin.

    PMID: 29258848 [PubMed - as supplied by publisher]