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Structure of Myosin VI/Tom1 complex reveals a cargo recognition mode of Myosin VI for tethering

Author

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  • Shichen Hu

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

  • Yujiao Guo

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

  • Yingli Wang

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

  • Ying Li

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

  • Tao Fu

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

  • Zixuan Zhou

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

  • Yaru Wang

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

  • Jianping Liu

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

  • Lifeng Pan

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

Abstract

Myosin VI plays crucial roles in diverse cellular processes. In autophagy, Myosin VI can facilitate the maturation of autophagosomes through interactions with Tom1 and the autophagy receptors, Optineurin, NDP52 and TAX1BP1. Here, we report the high-resolution crystal structure of the C-terminal cargo-binding domain (CBD) of Myosin VI in complex with Tom1, which elucidates the mechanistic basis underpinning the specific interaction between Myosin VI and Tom1, and uncovers that the C-terminal CBD of Myosin VI adopts a unique cargo recognition mode to interact with Tom1 for tethering. Furthermore, we show that Myosin VI can serve as a bridging adaptor to simultaneously interact with Tom1 and autophagy receptors through two distinct interfaces. In all, our findings provide mechanistic insights into the interactions of Myosin VI with Tom1 and relevant autophagy receptors, and are valuable for further understanding the functions of these proteins in autophagy and the cargo recognition modes of Myosin VI.

Suggested Citation

  • Shichen Hu & Yujiao Guo & Yingli Wang & Ying Li & Tao Fu & Zixuan Zhou & Yaru Wang & Jianping Liu & Lifeng Pan, 2019. "Structure of Myosin VI/Tom1 complex reveals a cargo recognition mode of Myosin VI for tethering," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11481-6
    DOI: 10.1038/s41467-019-11481-6
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    Cited by:

    1. Louise Canon & Carlos Kikuti & Vicente J. Planelles-Herrero & Tianming Lin & Franck Mayeux & Helena Sirkia & Young il Lee & Leila Heidsieck & Léonid Velikovsky & Amandine David & Xiaoyan Liu & Dihia M, 2023. "How myosin VI traps its off-state, is activated and dimerizes," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Fengfeng Niu & Lingxuan Li & Lei Wang & Jinman Xiao & Shun Xu & Yong Liu & Leishu Lin & Cong Yu & Zhiyi Wei, 2024. "Autoinhibition and activation of myosin VI revealed by its cryo-EM structure," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Janeska J. Jonge & Andreas Graw & Vasileios Kargas & Christopher Batters & Antonino F. Montanarella & Tom O’Loughlin & Chloe Johnson & Susan D. Arden & Alan J. Warren & Michael A. Geeves & John Kendri, 2024. "Motor domain phosphorylation increases nucleotide exchange and turns MYO6 into a faster and stronger motor," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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