β-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 β-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 α- and β-Catenins. The phosphorylation of tyrosine 142 may act as a switch from the transcriptional to the adhesive role of β-Catenin. Src family kinases can also phosphorylate tyrosine 86, 333, 489, and 654 in β-Catenin. Tyr-654 phosphorylation regulates β-Catenin binding to E-cadherin, while c-Abl phosphorylation of Tyr-489 decreases β-Catenin binding to N-Cadherin and leads to nuclear translocation and transcriptional activation. In addition, Tyr-333 phosphorylation is required for binding to the metabolic kinase, PKM2,and promotes nuclear accumulation of both proteins in gliomas.
Yang, W. et al. (2011) Nature. 480(7375):118-22.
Piedra, J. et al. (2003) Mol. Cell. Biol. 23(7):2287.
Roura, S. et al. (1999) J Biol Chem. 274(51) :36734.
*For more information, see UniProt Accession P35222
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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