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Papers In Press, published online ahead of print March 21, 2001
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Osaka 565-0871
Corresponding Author: ytakai{at}molbio.med.osaka-u.ac.jp
Gab-1 is a multiple docking protein that is tyrosine phosphorylated by receptor tyrosine kinases such as c-Met, the hepatocyte growth factor/scatter factor receptor, and the epidermal growth factor receptor. We have now demonstrated that cell-cell adhesion also induces the marked tyrosine phosphorylation of Gab-1, and that disruption of cell-cell adhesion results in its dephosphorylation. The anti-E-cadherin antibody decreased the cell-cell adhesion-dependent tyrosine phosphorylation of Gab-1, while the expression of E-cadherin specifically induced the tyrosine phosphorylation of Gab-1. A relatively selective inhibitor of Src family kinases reduced the cell-cell adhesion-dependent tyrosine phosphorylation of Gab-1, whereas expression of a dominant-negative mutant of Csk increased it. Disruption of cell-cell adhesion, that reduced the tyrosine phosphorylation of Gab-1, also reduced the activation of MAP kinase and Akt in response to cell-cell adhesion. These results indicate that the E-cadherin-mediated cell-cell adhesion induces the tyrosine phosphorylation by a Src family kinase of Gab-1, thereby regulating the activation of Ras/MAP kinase and PI 3-kinase/Akt cascades.
J. Biol. Chem, 10.1074/jbc.M100909200
Submitted on January 31, 2001
Revised on March 19, 2001
Accepted on March 20, 2001
Roles of cell-cell adhesion-dependent tyrosine phosphorylation of Gab-1
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