TORC2-Gad8-dependent myosin phosphorylation modulates regulation by calcium

Elife. 2019 Sep 30:8:e51150. doi: 10.7554/eLife.51150.

Abstract

Cells respond to changes in their environment through signaling networks that modulate cytoskeleton and membrane organization to coordinate cell-cycle progression, polarized cell growth and multicellular development. Here, we define a novel regulatory mechanism by which the motor activity and function of the fission yeast type one myosin, Myo1, is modulated by TORC2-signalling-dependent phosphorylation. Phosphorylation of the conserved serine at position 742 (S742) within the neck region changes both the conformation of the neck region and the interactions between Myo1 and its associating calmodulin light chains. S742 phosphorylation thereby couples the calcium and TOR signaling networks that are involved in the modulation of myosin-1 dynamics to co-ordinate actin polymerization and membrane reorganization at sites of endocytosis and polarised cell growth in response to environmental and cell-cycle cues.

Keywords: S. pombe; TORC2; calmodulin; cell biology; endocytosis; myosin; pombe.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological*
  • Calcium / metabolism*
  • Mechanistic Target of Rapamycin Complex 2 / metabolism*
  • Myosin Heavy Chains / chemistry
  • Myosin Heavy Chains / metabolism*
  • Phosphorylation
  • Protein Conformation
  • Protein Processing, Post-Translational*
  • Protein Serine-Threonine Kinases / metabolism*
  • Schizosaccharomyces / physiology*
  • Schizosaccharomyces pombe Proteins / chemistry
  • Schizosaccharomyces pombe Proteins / metabolism*
  • Signal Transduction

Substances

  • Schizosaccharomyces pombe Proteins
  • myo1 protein, S pombe
  • Gad8 protein, S pombe
  • Mechanistic Target of Rapamycin Complex 2
  • Protein Serine-Threonine Kinases
  • Myosin Heavy Chains
  • Calcium