beta-Catenin is a 92 kDa protein that binds to the cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions. Deletions in the cytoplasmic domain of E-Cadherin eliminate catenin binding and result in a loss of cell adhesion. Tyrosine phosphorylation of beta-Catenin can regulate its interaction with critical components of adherens junctions. Both Fer and Fyn kinases phosphorylate tyrosine 142 in vitro. Overexpression of these kinases in epithelial cells disrupts interactions between alpha- and beta-Catenins. The phosphorylation of tyrosine 142 may act as a switch from the transcriptional to the adhesive role of beta-Catenin. Src family kinases can also phosphorylate tyrosine 86 and 654 in beta-Catenin. The Tyr-654 phosphorylation regulates beta-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of beta-Catenin may regulate protein-protein interactions leading to changes in cell adhesion.
beta-Catenin is a 92 kDa protein that binds to the cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions. Deletions in the cytoplasmic domain of E-Cadherin eliminate catenin binding
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