Rho effectors and reorganization of actin cytoskeleton

FEBS Lett. 1997 Jun 23;410(1):68-72. doi: 10.1016/s0014-5793(97)00317-7.

Abstract

The small GTPase Rho regulates several actomyosin-based cellular processes such as cell adhesion, cytokinesis and contraction. The biochemical mechanisms of these actions remain unknown. Recently, several GTP-Rho binding proteins were isolated. Among them, p140mDia and p160ROCK appear to work as Rho effectors mediating its action on the cytoskeleton. p140mDia induces actin polymerization by recruiting an actin binding protein, profilin, to the site of Rho action. p160ROCK induces focal adhesions and stress fibers by activating integrin and clustering them by the use of myosin-based contractility.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism*
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / physiology*
  • GTP-Binding Proteins / metabolism*
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / isolation & purification
  • Protein-Serine-Threonine Kinases / physiology*
  • rho-Associated Kinases
  • rhoB GTP-Binding Protein

Substances

  • Actins
  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Protein-Serine-Threonine Kinases
  • rho-Associated Kinases
  • GTP-Binding Proteins
  • rhoB GTP-Binding Protein