Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion

FEBS Lett. 1994 Nov 28;355(2):195-200. doi: 10.1016/0014-5793(94)01205-9.


Catenins are peripheral cytoplasmic proteins originally identified in association with the mouse epithelial cell adhesion molecule E-cadherin. Molecular cloning and primary structure analysis demonstrated that alpha-catenin is homologous to vinculin and the beta-catenin is homologous to human plakoglobin and the Drosophila gene product armadillo. With the use of peptide-specific anti plakoglobin antibodies were confirm here that plakoglobin is a component of the cadherin-catenin complex and that it is most likely identical to gamma-catenin. We show that plakoglobin binds directly to E-cadherin. We consolidate the biochemical evidence for the existence of two distinct and separable E-cadherin-catenin complexes in the same cell. One complex is composed of E-cadherin, alpha- and beta-catenin, the other of E-cadherin, alpha-catenin and plakoglobin. A similar distinct association with catenins is also found for other cadherins. Comparison of different cell lines revealed that the relative amounts of the two complexes vary depending on cell types.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cadherins / metabolism*
  • Calcium / metabolism
  • Cattle
  • Cell Adhesion / physiology*
  • Cell Line
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Desmoplakins
  • Humans
  • Mice
  • Molecular Sequence Data
  • Octoxynol
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Solubility
  • Trans-Activators*
  • alpha Catenin
  • beta Catenin
  • gamma Catenin


  • CTNNA1 protein, human
  • CTNNB1 protein, human
  • CTNNB1 protein, mouse
  • Cadherins
  • Ctnna1 protein, mouse
  • Cytoskeletal Proteins
  • Desmoplakins
  • JUP protein, human
  • Jup protein, mouse
  • Peptide Fragments
  • Trans-Activators
  • alpha Catenin
  • beta Catenin
  • gamma Catenin
  • Octoxynol
  • Calcium