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

Biochemical Journal - Tập 360 Số 2 - Trang 335-344 - 2001
Richard Woodfield1, Matthew N. Hodgkin2, Nasreen Akhtar1, Mary A. Morse3, K J Fuller3, K M Saqib1, Neil T. Thompson3, Michael J.O. Wakelam1
1Institute for Cancer Studies, University of Birmingham, Edgbaston, Birmingham B15 2TA, U.K.
2Molecular Physiology Group, Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, U.K.
3Department of Immunology, GlaxoSmithKline Research and Development, Gunnels Wood Road, Stevenage SG1 2NY, U.K.

Tóm tắt

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 β-catenin. We also show that the interaction of p85 and β-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.

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Biochemical Journal

Tập 360 Số 2

335-344

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