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

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  • Weiyi Wang

    (Tongji University
    Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay)

  • 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)

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.

Suggested Citation

  • Weiyi Wang & Soraya Cantos-Fernandes & Yuncong Lv & Hureshitanmu Kuerban & Shoeb Ahmad & Chunguang Wang & Benoît Gigant, 2017. "Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin," Nature Communications, Nature, vol. 8(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00091-9
    DOI: 10.1038/s41467-017-00091-9
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    Cited by:

    1. Byron Hunter & Matthieu P. M. H. Benoit & Ana B. Asenjo & Caitlin Doubleday & Daria Trofimova & Corey Frazer & Irsa Shoukat & Hernando Sosa & John S. Allingham, 2022. "Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    2. Vladimir A Fedorov & Philipp S Orekhov & Ekaterina G Kholina & Artem A Zhmurov & Fazoil I Ataullakhanov & Ilya B Kovalenko & Nikita B Gudimchuk, 2019. "Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability," PLOS Computational Biology, Public Library of Science, vol. 15(8), pages 1-25, August.

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