The p85 subunit of PI-3-kinase is associated with β-catenin in the cadherin-based adhesion complex

Richard Woodfield, Matthew Hodgkin, N Akhtar, MA Morse, KJ Fuller, Khalid Saqib, NT Thompson, Michael Wakelam

Research output: Contribution to journalArticle

44 Citations (Scopus)


Cell adhesion is fundamental to establishing and maintaining the discrete tissues in multicellular organisms. Adhesion must be sufficiently strong to preserve tissue architecture, whilst having the capacity to readily dissociate to permit fundamental processes, such as wound repair, to occur. However, very little is known about the signalling mechanisms involved in temporary down-regulation of cell adhesion to facilitate such processes. Cadherins are the principal mediators of cell-cell adhesion in a wide variety of tissues and species and form multi-protein complexes with cytosolic and cytoskeletal proteins to express their full adhesive capacity. In the present study we report that the p85 subunit of phosphoinositide 3-kinase (PI 3-kinase) is associated with the cadherin-based adhesion complex in human epithelial cells. The interaction of p85 with the complex is via beta -catenin. We also show that the interaction of p85 and beta -catenin is direct, involves the N-terminal Src homology domain 2 of p85 and is regulated by tyrosine phosphorylation. These data suggest that PI 3-kinase may play a role in the functional regulation of the cadherin-based adhesion complex.
Original languageEnglish
Pages (from-to)335-344
Number of pages10
JournalBiochemical Journal
Issue number2
Publication statusPublished - 1 Dec 2001


  • epithelia
  • cell-cell adhesion
  • protein interactions
  • PI 3-kinase


Dive into the research topics of 'The p85 subunit of PI-3-kinase is associated with β-catenin in the cadherin-based adhesion complex'. Together they form a unique fingerprint.

Cite this