A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated

Cell Adhes Commun. 1994 Aug;2(4):319-27. doi: 10.3109/15419069409014207.


Classical cadherins associate with three cytoplasmic proteins, termed alpha, -beta- and gamma-catenin. This association mediates the attachment of cadherins to the microfilament network, which is believed to be of major importance for cadherin function. Deletion of the carboxyterminal 72-amino acid residues of E-cadherin had been previously shown to prevent catenin binding. Here we have analyzed additional mutants of E-cadherin with deletions within this region and identified a core region of 30 amino acids (E-cadherin pos. 832-862) essential for the interaction with catenins. Phosphorylation analysis of wild-type and mutant E-cadherin indicates that the catenin-binding domain is highly phosphorylated. In particular, the 30 amino acid region contains 8 serine residues which are well conserved among cadherins. To elucidate whether phosphorylation might be important for cadherin-catenin complex formation, site-directed mutagenesis experiments were performed. Partial substitutions of up to 5 of the 8 serine residues in the cluster had no influence on E-cadherin-catenin complex formation and E-cadherin mediated cell adhesion, although phosphorylation of E-cadherin was reduced. In contrast, substitution of the whole serine cluster completely abolished phosphorylation and affected complex formation with catenins. These results suggest that E-cadherin-catenin interaction may be regulated by phosphorylation of the catenin-binding domain, which might represent one molecular mechanism to regulate cadherin mediated cell adhesion.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Cadherins / genetics
  • Cadherins / metabolism*
  • Cell Aggregation
  • Conserved Sequence
  • Cytoskeletal Proteins / metabolism*
  • Desmoplakins
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Sequence Deletion / physiology
  • Serine / physiology
  • Trans-Activators*
  • alpha Catenin
  • beta Catenin
  • gamma Catenin


  • Cadherins
  • Cytoskeletal Proteins
  • Desmoplakins
  • Trans-Activators
  • alpha Catenin
  • beta Catenin
  • gamma Catenin
  • Serine