alpha-catenins are cadherin interacting proteins with homology to vinculin. Three alpha-catenin genes have been described including alpha1-catenin (alphaE-Catenin), alpha2-catenin (alphaN-catenin), and alpha3-catenin (alphaT-catenin). alpha1-catenin has 81% homology with alpha2-catenin and 60% homology with alpha3-catenin. These alpha-catenin isoforms may have similar roles since each binds cadherins. However, their expression patterns are both overlapping and distinct. alpha1-catenin was identified in epithelial cells, and is expressed in various cell types. alpha2-catenin is enriched in the nervous system, and alpha3-catenin is expressed highest in testis and heart. Phosphorylation may regulate the activity of alpha1-catenin, since tyrosine phosphorylation of Tyr-148 occurs during intercellular adhesion. This site is dephosphorylated by SHP2, which inhibits alpha1-catenin binding to beta-catenin and translocation to the plasma membrane. Phosphorylation of alpha1-catenin at Tyr-148 may be important for inhibition of cell transformation, and dephosphorylation of this site may be important during SHP2-mediated cell transformation.
alpha-catenins are cadherin interacting proteins with homology to vinculin. Three alpha-catenin genes have been described including alpha1-catenin (alphaE-Catenin), alpha2-catenin (alphaN-catenin), and alpha3-catenin (alphaT-catenin). alpha1-catenin has 8
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