From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion

Trends Genet. 1993 Sep;9(9):317-21. doi: 10.1016/0168-9525(93)90250-l.


Classical cadherins are complexed via their cytoplasmic domains with alpha-, beta- and gamma-catenin. This complex formation links cadherins to the actin filament network and to other transmembrane and cytoplasmic proteins. alpha-Catenin is homologous to vinculin, and beta-catenin to the product of the Drosophila gene armadillo, while gamma-catenin seems to be identical to plakoglobin. Catenins are part of a higher order protein structure that is of crucial importance for the adhesive function of cadherins. A working model of the construction and regulation of this multiprotein interaction is proposed.

Publication types

  • Review

MeSH terms

  • Actins / metabolism
  • Animals
  • Cadherins / chemistry
  • Cadherins / physiology*
  • Cell Adhesion / physiology*
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / physiology*
  • Cytoplasm / metabolism
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / physiology*
  • Desmoplakins
  • Drosophila melanogaster / genetics
  • Humans
  • Mice
  • Models, Biological
  • Trans-Activators*
  • alpha Catenin
  • beta Catenin
  • gamma Catenin


  • Actins
  • CTNNA1 protein, human
  • CTNNB1 protein, human
  • CTNNB1 protein, mouse
  • Cadherins
  • Cell Adhesion Molecules
  • Ctnna1 protein, mouse
  • Cytoskeletal Proteins
  • Desmoplakins
  • JUP protein, human
  • Jup protein, mouse
  • Trans-Activators
  • alpha Catenin
  • beta Catenin
  • gamma Catenin