Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
| Autor: | Wang, Weiyi, Cantos-Fernandes, Soraya, Lv, Yuncong, Kuerban, Hureshitanmu, Ahmad, Shoeb, Wang, Chunguang, Gigant, Benoît |
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| Přispěvatelé: | Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institute of Protein Research, Tong Ji University |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Adenosine Triphosphatases
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Protein Conformation Science Kinesins [SDV.BC]Life Sciences [q-bio]/Cellular Biology macromolecular substances Microtubules Gene Expression Regulation Enzymologic Article Mutation Escherichia coli [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Crystallization |
| Zdroj: | Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017) 'Nature Communications ', vol: 8, pages: 70-1-70-11 (2017) Nature Communications Nature Communications, Nature Publishing Group, 2017, 8 (1), pp.70. ⟨10.1038/s41467-017-00091-9⟩ Nature Communications, 2017, 8 (1), pp.70. ⟨10.1038/s41467-017-00091-9⟩ |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-017-00091-9⟩ |
| Popis: | Kinesin-13s are critical microtubule regulators which induce microtubule disassembly in an ATP dependent manner. To clarify their mechanism, we report here the crystal structure of a functional construct of the kinesin-13 Kif2C/MCAK in an ATP-like state and bound to the αβ-tubulin heterodimer, a complex mimicking the species that dissociates from microtubule ends during catalytic disassembly. Our results picture how Kif2C stabilizes a curved tubulin conformation. The Kif2C α4-L12-α5 region undergoes a remarkable 25° rotation upon tubulin binding to target the αβ-tubulin hinge. This movement leads the β5a–β5b motif to interact with the distal end of β-tubulin, whereas the neck and the KVD motif, two specific elements of kinesin-13s, target the α-tubulin distal end. Taken together with the study of Kif2C mutants, our data suggest that stabilization of a curved tubulin is an important contribution to the Kif2C mechanism. Kinesin-13s are microtubule depolymerizing enzymes. Here the authors present the crystal structure of a DARPin fused construct comprising the short neck region and motor domain of kinesin-13 in complex with an αβ-tubulin heterodimer, which shows that kinesin-13 functions by stabilizing a curved tubulin conformation. |
| Databáze: | OpenAIRE |
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