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Myosin Vs organize actin cables in fission yeast.

Myosin V motors are believed to contribute to cell polarization by carrying cargoes along actin tracks. In Schizosaccharomyces pombe, Myosin Vs transport secretory vesicles along actin cables, which are dynamic actin bundles assembled by the formin For3 at cell poles. How these flexible structures are able to extend longitudinally in the cell through the dense cytoplasm is unknown. Here we show that in myosin V (myo52 myo51) null cells, actin cables are curled, bundled, and fail to extend into the cell interior. They also exhibit reduced retrograde flow, suggesting that formin-mediated actin assembly is impaired. Myo52 may contribute to actin cable organization by delivering actin regulators to cell poles, as myoV defects are partially suppressed by diverting cargoes toward cell tips onto microtubules with a kinesin 7-Myo52 tail chimera. In addition, Myo52 motor activity may pull on cables to provide the tension necessary for their extension and efficient assembly, as artificially tethering actin cables to the nuclear envelope via a Myo52 motor domain restores actin cable extension and retrograde flow in myoV mutants. Together these in vivo data reveal elements of a self-organizing system in which the motors shape their own tracks by transporting cargoes and exerting physical pulling forces.

Pubmed ID: 23051734


  • Lo Presti L
  • Chang F
  • Martin SG


Molecular biology of the cell

Publication Data

December 30, 2012

Associated Grants

  • Agency: European Research Council, Id: 260493
  • Agency: NIGMS NIH HHS, Id: GM05636
  • Agency: NIGMS NIH HHS, Id: R01 GM0669670

Mesh Terms

  • Actin Cytoskeleton
  • Actins
  • Cell Cycle Proteins
  • Cell Polarity
  • Cytoplasm
  • Kinesin
  • Microtubules
  • Myosin Type V
  • Myosins
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Secretory Vesicles