UNSPECIFIED (2001) The p85 subunit of phosphoinositide 3-kinase is associated with beta-catenin in the cadherin-based adhesion complex. BIOCHEMICAL JOURNAL, 360 (Part 2). pp. 335-344. ISSN 0264-6021

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Abstract

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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	BIOCHEMICAL JOURNAL
Publisher:	PORTLAND PRESS
ISSN:	0264-6021
Date:	1 December 2001
Volume:	360
Number:	Part 2
Number of Pages:	10
Page Range:	pp. 335-344
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/11408

Data sourced from Thomson Reuters' Web of Knowledge

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