Controversies at the Cytoplasmic Face of the Cadherin-Based Adhesion Complex

Curr Opin Cell Biol. 1999 Oct;11(5):567-72. doi: 10.1016/s0955-0674(99)00015-0.

Abstract

Cadherin-mediated cell-cell interactions are modulated by protein interactions at the cytoplasmic face of the membrane. Recent work has shown that phosphorylation of both p120(ctn) and beta-catenin affects their interaction with cadherins and the molecular connections to the cytoskeleton. The cytoskeletal connections most probably include interactions between alpha-catenin, and/or alpha-actinin, vinculin, ZO-1, actin and possibly spectrin.

Publication types

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

MeSH terms

  • Animals
  • Armadillo Domain Proteins
  • Cadherins / chemistry
  • Cadherins / physiology*
  • Calcium / metabolism
  • Catenins
  • Cell Adhesion / physiology*
  • Cell Adhesion Molecules / metabolism
  • Cytoplasm / ultrastructure*
  • Cytoskeletal Proteins / metabolism
  • Dimerization
  • Drosophila Proteins*
  • Humans
  • Insect Proteins / chemistry
  • Macromolecular Substances
  • Multigene Family
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Spectrin / metabolism
  • Trans-Activators*
  • Vinculin / metabolism
  • alpha Catenin
  • beta Catenin

Substances

  • Armadillo Domain Proteins
  • CTNNA1 protein, human
  • CTNNB1 protein, human
  • Cadherins
  • Catenins
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • Drosophila Proteins
  • Insect Proteins
  • Macromolecular Substances
  • Phosphoproteins
  • Trans-Activators
  • alpha Catenin
  • beta Catenin
  • delta catenin
  • Vinculin
  • Spectrin
  • Calcium