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

Weiyi Wang, Soraya Cantos-Fernandes, Yuncong Lv, Hureshitanmu Kuerban, Shoeb Ahmad, Chunguang Wang () and Benoît Gigant ()
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Weiyi Wang: Tongji University
Soraya Cantos-Fernandes: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay
Yuncong Lv: Tongji University
Hureshitanmu Kuerban: Tongji University
Shoeb Ahmad: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay
Chunguang Wang: Tongji University
Benoît Gigant: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/s41467-017-00091-9

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