Evidence that the V832M E-Cadherin germ-line missense mutation does not influence the affinity of α-catenin for the cadherin/catenin complex

Matthew W. Curtis, Quan P. Ly, Margaret J. Wheelock, Keith R. Johnson

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Mutations in E-cadherin are associated with a number of diseases, and have been shown to contribute to disease progression. In particular, 50% of hereditary diffuse gastric cancer cases have inactivating mutations in the E-cadherin gene. An interesting mutation near the beta-catenin-binding site on the cytoplasmic domain of E-cadherin (V832M) was recently reported that produces full-length protein, but exhibits decreased binding of α -catenin to the cadherin/catenin complex. The study was done by transfecting mutant E-cadherin into Chinese hamster ovary fibroblast cells. Here we show that the previously reported characteristics of this mutation do not apply to human epithelial cells expressing this mutant protein and suggest that the mechanism whereby the V832M mutation in human E-cadherin promotes gastric cancer is not yet understood.

Original languageEnglish (US)
Pages (from-to)45-55
Number of pages11
JournalCell Communication and Adhesion
Volume14
Issue number2-3
DOIs
StatePublished - Mar 2007

Keywords

  • Cadherin
  • Cadherin/catenin complex
  • Cell adhesion
  • α-catenin

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology

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