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The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A

Nature Reviews Molecular Cell Biology volume 10, pages 877–884 (2009)Cite this article

Abstract

Most kinesins move processively along microtubules by using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin 3 family motor KIF1A. Based on this structural information, we propose a common mechanism of kinesin motility, focusing on the regulation of kinesin motility through their interaction with microtubules and by their 'neck-linker' region, which connects their motor domain to cargo and kinesin partner heads.

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Figure 1: Structure and motility models of KIF5 and KIF1A.
Figure 2: Atomic mechanism of KIF1A nucleotide exchange.
Figure 3: Three-step docking of the neck linker.
Figure 4: Structural model of KIF1A and its application to the hand-over-hand model for KIF5.

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Acknowledgements

We thank Keiko Hirose for cryo-electron microscopy maps of kar3 and members of the Hirokawa laboratory for assistance and discussion. This work was supported by the Ministry of Education, Culture, Sports, Science and Technology of Japan, Grant-in-Aid for Specially Promoted Research to N.H.

Author information

Authors and Affiliations

  1. Ryo Nitta and Yasushi Okada are at the Department of Cell Biology and Anatomy, Nobutaka Hirokawa, University of Tokyo, Graduate School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.,

    Nobutaka Hirokawa, Ryo Nitta & Yasushi Okada

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  1. Nobutaka Hirokawa
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Correspondence to Nobutaka Hirokawa.

Supplementary information

Supplementary information S1 (movie) | Overview of the atomic structure of kinesin motor domain. (SWF 8384 kb)

41580_2009_BFnrm2807_MOESM2_ESM.pdf

Supplementary information S2 (movie) | Conformation changes of KIF1A during the ATPase reaction cycle. (SWF 583 kb)

41580_2009_BFnrm2807_MOESM4_ESM.pdf

Supplementary information S3 (movie) | Coupling between switch I and switch II during the ATPase cycle. (SWF 7400 kb)

41580_2009_BFnrm2807_MOESM6_ESM.pdf

41580_2009_BFnrm2807_MOESM7_ESM.pdf

Supplementary information S4 (figure) | Conserved role of loop L7 as the trigger for the microtubule activation of Mg-ADP release. (PDF 453 kb)

Supplementary information S5 (movie) | Structure-based model of the 'ATP gating' of dimeric kinesin. (MOV 6316 kb)

41580_2009_BFnrm2807_MOESM9_ESM.pdf

Supplementary information S6 (movie) | Structural model of the monomeric motility of KIF1A. (MOV 6823 kb)

41580_2009_BFnrm2807_MOESM11_ESM.pdf

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Hirokawa, N., Nitta, R. & Okada, Y. The mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A. Nat Rev Mol Cell Biol 10, 877–884 (2009). https://doi.org/10.1038/nrm2807

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