Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover

Mol Biol Cell. 2014 Oct 1;25(19):3006-16. doi: 10.1091/mbc.E14-05-0965. Epub 2014 Aug 7.


The growth of fission yeast relies on the polymerization of actin filaments nucleated by formin For3p, which localizes at tip cortical sites. These actin filaments bundle to form actin cables that span the cell and guide the movement of vesicles toward the cell tips. A big challenge is to develop a quantitative understanding of these cellular actin structures. We used computer simulations to study the spatial and dynamical properties of actin cables. We simulated individual actin filaments as semiflexible polymers in three dimensions composed of beads connected with springs. Polymerization out of For3p cortical sites, bundling by cross-linkers, pulling by type V myosin, and severing by cofilin are simulated as growth, cross-linking, pulling, and turnover of the semiflexible polymers. With the foregoing mechanisms, the model generates actin cable structures and dynamics similar to those observed in live-cell experiments. Our simulations reproduce the particular actin cable structures in myoVΔ cells and predict the effect of increased myosin V pulling. Increasing cross-linking parameters generates thicker actin cables. It also leads to antiparallel and parallel phases with straight or curved cables, consistent with observations of cells overexpressing α-actinin. Finally, the model predicts that clustering of formins at cell tips promotes actin cable formation.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actin Depolymerizing Factors / metabolism
  • Actinin / biosynthesis
  • Cell Cycle Proteins / metabolism*
  • Formins
  • Molecular Dynamics Simulation*
  • Myosin Type V / metabolism
  • Schizosaccharomyces / growth & development*
  • Schizosaccharomyces pombe Proteins / metabolism*


  • Actin Depolymerizing Factors
  • Cell Cycle Proteins
  • FOR3 protein, S pombe
  • Formins
  • Schizosaccharomyces pombe Proteins
  • Actinin
  • Myosin Type V