c-erbB-2 gene product associates with catenins in human cancer cells

Biochem Biophys Res Commun. 1994 Nov 30;205(1):73-8. doi: 10.1006/bbrc.1994.2631.


Phosphorylation of beta-catenin, an intracytoplasmic cadherin-binding protein, causes disruption of the cadherin-mediated cell adhesion system in cancer cells. A 185-kDa phosphorylated protein, identified as the c-erbB-2 gene product, was co-immunoprecipitated with the E-cadherin-catenin complex. Association of the c-erbB-2 gene product with the cadherin-catenin complex was proven to be mediated through beta-catenin and plakoglobin using an in vitro protein-protein precipitation system. These results indicate that the c-erbB-2 gene product associates with catenins and may regulate the cell adhesion and invasive growth of cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cadherins / metabolism*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • Desmoplakins
  • Escherichia coli / genetics
  • Humans
  • Phosphorylation
  • Receptor, ErbB-2 / genetics
  • Receptor, ErbB-2 / metabolism*
  • Trans-Activators*
  • Tumor Cells, Cultured
  • beta Catenin
  • gamma Catenin


  • CTNNB1 protein, human
  • Cadherins
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • Desmoplakins
  • Trans-Activators
  • beta Catenin
  • gamma Catenin
  • Receptor, ErbB-2