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The myosin X motor is optimized for movement on actin bundles

Author

Listed:
  • Virginie Ropars

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

  • Zhaohui Yang

    (University of Florida College of Medicine)

  • Tatiana Isabet

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

  • Florian Blanc

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD
    Laboratoire d'Ingénierie des Fonctions Moléculaires (ISIS), UMR 7006 CNRS, Université de Strasbourg)

  • Kaifeng Zhou

    (Yale University)

  • Tianming Lin

    (University of Florida College of Medicine)

  • Xiaoyan Liu

    (University of Florida College of Medicine)

  • Pascale Hissier

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

  • Frédéric Samazan

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

  • Béatrice Amigues

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

  • Eric D. Yang

    (University of Florida College of Medicine)

  • Hyokeun Park

    (and State Key Laboratory of Molecular Neuroscience. The Hong Kong University of Science and Technology)

  • Olena Pylypenko

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

  • Marco Cecchini

    (Laboratoire d'Ingénierie des Fonctions Moléculaires (ISIS), UMR 7006 CNRS, Université de Strasbourg)

  • Charles V. Sindelar

    (Yale University)

  • H. Lee Sweeney

    (University of Florida College of Medicine)

  • Anne Houdusse

    (Structural Motility, Institut Curie, PSL Research University, CNRS
    Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD)

Abstract

Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles.

Suggested Citation

  • Virginie Ropars & Zhaohui Yang & Tatiana Isabet & Florian Blanc & Kaifeng Zhou & Tianming Lin & Xiaoyan Liu & Pascale Hissier & Frédéric Samazan & Béatrice Amigues & Eric D. Yang & Hyokeun Park & Olen, 2016. "The myosin X motor is optimized for movement on actin bundles," Nature Communications, Nature, vol. 7(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12456
    DOI: 10.1038/ncomms12456
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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.

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