Regulation and control of myosin-I by the motor and light chain-binding domains

Trends Cell Biol. 2013 Feb;23(2):81-9. doi: 10.1016/j.tcb.2012.10.008. Epub 2012 Nov 29.

Abstract

Members of the myosin-I family of molecular motors are expressed in many eukaryotes, where they are involved in a multitude of critical processes. Humans express eight distinct members of the myosin-I family, making it the second largest family of myosins expressed in humans. Despite the high degree of sequence conservation in the motor and light chain-binding domains (LCBDs) of these myosins, recent studies have revealed surprising diversity of function and regulation arising from isoform-specific differences in these domains. Here we review the regulation of myosin-I function and localization by the motor and LCBDs.

Publication types

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

MeSH terms

  • Actins / chemistry
  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphate / chemistry
  • Animals
  • Binding Sites
  • Biomechanical Phenomena
  • Cell Membrane / chemistry*
  • Humans
  • Mechanotransduction, Cellular*
  • Myosin Type I / chemistry*
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Isoforms / chemistry
  • Protein Structure, Tertiary
  • Protein Transport

Substances

  • Actins
  • Protein Isoforms
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • Myosin Type I
  • MYO1C protein, human