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Papers In Press, published online ahead of print July 18, 2005
Department of Pathology, Moores Cancer Center, University of California at San Diego, La Jolla, CA 92093-0803
Corresponding Author: dcheresh{at}ucsd.edu
In several pathological conditions, epithelial cells demonstrate a breakdown of barrier function and acquire an invasive phenotype. Endothelial cells in particular are maintained in a mesenchymal state during the cell invasion phase of angiogenesis. We show here that tyrosine phosphorylation of the adherens junction protein VE-cadherin at two critical tyrosines, Y658 and Y731, via tyrosine kinase activation or phosphatase inactivation, was sufficient to prevent the binding of p120- and
J. Biol. Chem, 10.1074/jbc.M505568200
Submitted on May 20, 2005
Revised on July 8, 2005
Accepted on July 18, 2005
Tyrosine phosphorylation of VE-cadherin prevents binding of p120- and
-catenins and maintains the cellular mesenchymal state
-catenins to the cytoplasmic tail of VE-cadherin, respectively. In fact, phosphorylation at either site lead to the inhibition of cell barrier function. Cells expressing wild-type VE-cadherin showed decreased cell migration compared to cells lacking VE-cadherin, whereas expression of VE-cadherin with a simple phospho-mimetic tyrosine-to-glutamic acid mutation of Y658E or Y731E was sufficient to restore the migratory response. These findings demonstrate that a single phosphorylation event within the VE-cadherin cytoplasmic tail is sufficient to maintain cells in a mesenchymal state.
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