E-Cadherin negatively modulates delta-catenin-induced morphological changes and RhoA activity reduction by competing with p190RhoGEF for delta-catenin

Biochem Biophys Res Commun. 2008 Dec 12;377(2):636-641. doi: 10.1016/j.bbrc.2008.10.030. Epub 2008 Oct 16.

Abstract

delta-Catenin is a member of the p120-catenin subfamily of armadillo proteins. Here, we describe distinctive features of delta-catenin localization and its association with E-cadherin in HEK293 epithelial cells. In HEK293 cells maintained in low cell densities, approximately 15% of cells overexpressing delta-catenin showed dendrite-like process formation, but there was no detectable change in RhoA activity. In addition, delta-catenin was localized mainly in the cytoplasm and was associated with p190RhoGEF. However, at high cell densities, delta-catenin localization was shifted to the plasma membrane. The association of delta-catenin with E-cadherin was strengthened, whereas its interaction with p190RhoGEF was weakened. In mouse embryonic fibroblast cell, ectopic expression of E-cadherin decreased the effect of delta-catenin on the reduction of RhoA activity as well as on dendrite-like process formation. These results suggest that delta-catenin is more dominantly bound to E-cadherin than to p190RhoGEF, and that delta-catenin's function is dependent on its cellular binding partner.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cadherins / metabolism*
  • Catenins
  • Cell Adhesion Molecules / metabolism*
  • Cell Line
  • Cytoplasm / metabolism
  • Humans
  • Mice
  • NIH 3T3 Cells
  • Phosphoproteins / metabolism*
  • ras-GRF1 / metabolism*
  • rhoA GTP-Binding Protein / metabolism*

Substances

  • Cadherins
  • Catenins
  • Cell Adhesion Molecules
  • Phosphoproteins
  • delta catenin
  • ras-GRF1
  • rhoA GTP-Binding Protein