p120-catenin is a key component of the cadherin-γ-secretase supercomplex

Alexi Kiss, Regina B. Troyanovsky, Sergey M. Troyanovsky

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

In this work, we show several previously unknown features of p120-catenin in a cadherin-catenin complex that are critical for our understanding of cadherin-based adhesion and signaling. We show that in human epithelial A-431 cells, nearly all p120 molecules engage in high-affinity interaction with E-cadherin-catenin complexes located at the cellular surface. p120 is positioned in proximity to α-catenin in the complex with cadherin. These findings suggest a functional cooperation between p120 and α-catenin in cadherin-based adhesion. A low level of cadherin-free p120 molecules, in contrast, could facilitate p120-dependent signaling. Finally, we present compelling evidence that p120 is a key linker cementing the E-cadherin-catenin complex with the transmembrane protease γ-secretase. The cell-cell contact location of this super-complex makes it an important candidate for conducting different signals that rely on γ-secretase proteolytic activity.

Original languageEnglish (US)
Pages (from-to)4042-4050
Number of pages9
JournalMolecular biology of the cell
Volume19
Issue number10
DOIs
StatePublished - Oct 1 2008

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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