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The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition

Author

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  • Wenjuan Wang

    (Chinese Academy of Sciences)

  • Jinqi Ren

    (Chinese Academy of Sciences)

  • Weiye Song

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Yong Zhang

    (Chinese Academy of Sciences)

  • Wei Feng

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

Abstract

Autoinhibition of kinesin-3 ensures the proper spatiotemporal control of the motor activity for intracellular transport, but the underlying mechanism remains elusive. Here, we determine the full-length structure of kinesin-3 KLP-6 in a compact self-folded state. Unexpectedly, all the internal coiled-coil segments and domains in KLP-6 cooperate to successively lock down the neck and motor domains. The first coiled-coil segment is melted into several short helices that work with the motor domain to restrain the entire neck domain. The second coiled-coil segment associates with its neighboring FHA and MBS domains and integrates with the tail MATH domain to form a supramodule that synergistically wraps around the motor domain to trap the nucleotide and hinder the microtubule binding. This multilevel-lockdown mechanism for autoinhibition could be applicable to other kinesin-3 motors.

Suggested Citation

  • Wenjuan Wang & Jinqi Ren & Weiye Song & Yong Zhang & Wei Feng, 2022. "The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32048-y
    DOI: 10.1038/s41467-022-32048-y
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    References listed on IDEAS

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    1. Nida Siddiqui & Alexander James Zwetsloot & Alice Bachmann & Daniel Roth & Hamdi Hussain & Jonathan Brandt & Irina Kaverina & Anne Straube, 2019. "PTPN21 and Hook3 relieve KIF1C autoinhibition and activate intracellular transport," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
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    Cited by:

    1. Chunting Zhang & Changmiao Guo & Ryan W. Russell & Caitlin M. Quinn & Mingyue Li & John C. Williams & Angela M. Gronenborn & Tatyana Polenova, 2022. "Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Xiangyu Fan & Richard J. McKenney, 2023. "Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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