Inhibition of RhoA by p120 catenin

Nat Cell Biol. 2000 Sep;2(9):637-44. doi: 10.1038/35023588.

Abstract

RhoA organizes actin stress fibres and is necessary for cell transformation by oncogenes such as src and ras. Moreover, RhoA is implicated in cadherin clustering during the formation of adherens junctions. The catenin p120 has also been implicated in cadherin clustering through an unknown mechanism. Here we show that p120 selectively inhibits RhoA activity in vitro and in vivo. RhoA inhibition and the interaction of p120 with cadherins are mutually exclusive, suggesting a mechanism for regulating the recruitment and exchange of RhoA at nascent cell-cell contacts. By affecting RhoA activation, p120 could modulate cadherin functions, including suppression of invasion, neurite extension and junction formation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Animals
  • Cadherins / metabolism
  • Catenins
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Guanosine Diphosphate / metabolism
  • Humans
  • Lysophospholipids / pharmacology
  • Mice
  • Phenotype
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Tumor Cells, Cultured
  • cdc42 GTP-Binding Protein / biosynthesis
  • cdc42 GTP-Binding Protein / genetics
  • rac1 GTP-Binding Protein / biosynthesis
  • rac1 GTP-Binding Protein / genetics
  • rhoA GTP-Binding Protein / antagonists & inhibitors*
  • rhoA GTP-Binding Protein / genetics
  • rhoA GTP-Binding Protein / metabolism

Substances

  • Cadherins
  • Catenins
  • Cell Adhesion Molecules
  • Lysophospholipids
  • Phosphoproteins
  • delta catenin
  • Guanosine Diphosphate
  • cdc42 GTP-Binding Protein
  • rac1 GTP-Binding Protein
  • rhoA GTP-Binding Protein