The myosin X motor is optimized for movement on actin bundles

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, Olena Pylypenko, Marco Cecchini, Charles V. Sindelar (), H. Lee Sweeney () and Anne Houdusse ()
Additional contact information
Virginie Ropars: Structural Motility, Institut Curie, PSL Research University, CNRS
Zhaohui Yang: University of Florida College of Medicine
Tatiana Isabet: Structural Motility, Institut Curie, PSL Research University, CNRS
Florian Blanc: Structural Motility, Institut Curie, PSL Research University, CNRS
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
Frédéric Samazan: Structural Motility, Institut Curie, PSL Research University, CNRS
Béatrice Amigues: Structural Motility, Institut Curie, PSL Research University, CNRS
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
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

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms12456

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