Structural Biochemistry of Microtubules,
Kinesins and their Cargos

Publications
3888256
MIKICA
1
chicago-author-date
50
date
desc
year
14268
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Iyer, Saishree S., Fangrui Chen, Funso E. Ogunmolu, Shoeib Moradi, Vladimir A. Volkov, Emma J. van Grinsven, Chris van Hoorn, et al. 2025. “Centriolar Cap Proteins CP110 and CPAP Control Slow Elongation of Microtubule plus Ends.” The Journal of Cell Biology 224 (3): e202406061. https://doi.org/10.1083/jcb.202406061.
Vargová, Romana, Roxanne Chevreau, Marine Alves, Camille Courbin, Kara Terry, Pierre Legrand, Marek Eliáš, Julie Ménétrey, Joel B. Dacks, and Catherine L. Jackson. 2025. “The Asgard Archaeal Origins of Arf Family GTPases Involved in Eukaryotic Organelle Dynamics.” Nature Microbiology, January. https://doi.org/10.1038/s41564-024-01904-6.
Vilela, Fernando, Cécile Sauvanet, Armel Bezault, Niels Volkmann, and Dorit Hanein. 2024. “Optimizing Transmembrane Protein Assemblies in Nanodiscs for Structural Studies: A Comprehensive Manual.” Bio-Protocol 14 (21): e5099. https://doi.org/10.21769/BioProtoc.5099.
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.
Jackson, Catherine L., Julie Ménétrey, Mandeep Sivia, Joel B. Dacks, and Marek Eliáš. 2023. “An Evolutionary Perspective on Arf Family GTPases.” Current Opinion in Cell Biology 85 (December):102268. https://doi.org/10.1016/j.ceb.2023.102268.
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.
Wang, Xingyu, Benoît Gigant, Xi Zheng, and Qiang Chen. 2023. “Microtubule‐targeting Agents for Cancer Treatment: Seven Binding Sites and Three Strategies.” MedComm – Oncology 2 (3): n/a-n/a. https://doi.org/10.1002/mog2.46.
Miller, Jessalyn, Agathe Urvoas, Benoit Gigant, Malika Ouldali, Ana Arteni, Agnes Mesneau, Marie Valerio-Lepiniec, Franck Artzner, Erik Dujardin, and Philippe Minard. 2023. “Engineering of Brick and Staple Components for Ordered Assembly of Synthetic Repeat Proteins.” Journal of Structural Biology 215 (3): 108012. https://doi.org/10.1016/j.jsb.2023.108012.
Monteiro-Cardoso, Vera F., Leila Rochin, Amita Arora, Audrey Houcine, Eeva Jääskeläinen, Annukka M. Kivelä, Cécile Sauvanet, et al. 2022. “ORP5/8 and MIB/MICOS Link ER-Mitochondria and Intra-Mitochondrial Contacts for Non-Vesicular Transport of Phosphatidylserine.” Cell Reports 40 (12). https://doi.org/10.1016/j.celrep.2022.111364.
Guyard, Valentin, Vera Filipa Monteiro-Cardoso, Mohyeddine Omrane, Cécile Sauvanet, Audrey Houcine, Claire Boulogne, Kalthoum Ben Mbarek, et al. 2022. “ORP5 and ORP8 Orchestrate Lipid Droplet Biogenesis and Maintenance at ER–Mitochondria Contact Sites.” Journal of Cell Biology 221 (9): e202112107. https://doi.org/10.1083/jcb.202112107.
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.
“Optimizing Transmembrane Protein Assemblies in Nanodiscs for Structural Studies: A Comprehensive Manual.” n.d. Accessed March 17, 2025. https://bio-protocol.org/en/bpdetail?id=5099&type=0.