2. Academic Validation
  3. The myosin X motor is optimized for movement on actin bundles

The myosin X motor is optimized for movement on actin bundles

  • Nat Commun. 2016 Sep 1;7:12456. doi: 10.1038/ncomms12456.
Virginie Ropars 1 2,  Zhaohui Yang 3,  Tatiana Isabet 1 2,  Florian Blanc 1 2 4,  Kaifeng Zhou 5,  Tianming Lin 3,  Xiaoyan Liu 3,  Pascale Hissier 1 2,  Frédéric Samazan 1 2,  Béatrice Amigues 1 2,  Eric D Yang 3,  Hyokeun Park 6,  Olena Pylypenko 1 2,  Marco Cecchini 4,  Charles V Sindelar 5,  H Lee Sweeney 3,  Anne Houdusse 1 2
Affiliations

Affiliations

  • 1 Structural Motility, Institut Curie, PSL Research University, CNRS, UMR 144, F-75005 Paris, France.
  • 2 Sorbonne Universités, UPMC Univ Paris 06, Sorbonne Universités, IFD, 4 Place Jussieu, 75252 Paris, France.
  • 3 Department of Pharmacology and Therapeutics and the Myology Institute, University of Florida College of Medicine, PO Box 100267, Gainesville, Florida 32610-0267, USA.
  • 4 Laboratoire d'Ingénierie des Fonctions Moléculaires (ISIS), UMR 7006 CNRS, Université de Strasbourg, F-67083 Strasbourg Cedex, France.
  • 5 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
  • 6 Department of Physics, Division of Life Science, and State Key Laboratory of Molecular Neuroscience. The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong.
PMID: 27580874 DOI: 10.1038/ncomms12456
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.

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