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Article Dans Une Revue Nature Communications Année : 2017

Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin

Résumé

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.
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Dates et versions

hal-02123770 , version 1 (25-01-2024)

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Weiyi Wang, Soraya Cantos-Fernandes, Yuncong Lv, Hureshitanmu Kuerban, Shoeb Ahmad, et al.. Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin. Nature Communications, 2017, 8, pp.70. ⟨10.1038/s41467-017-00091-9⟩. ⟨hal-02123770⟩
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