Plakoglobin (γ-Catenin) is a catenin family member identified as a component of desmosomes. γ-Catenin has high homology to β-catenin and, like β-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. One molecule of α-catenin and at least one molecule of β-catenin and γ-Catenin simultaneously bind to a single cadherin molecule. A 19-amino acid sequence of desmoglein was found to be critical for binding of γ-Catenin. Similar catenin-binding domains found in cadherins, suggest a common mechanism for γ-Catenin localization to both adherens junctions and desmosomes. Phosphorylation of tyrosine residues in γ-Catenin can modify its interactions with other proteins. Phosphorylation of tyrosine 644 decreases γ-Catenin association with α-catenin, but increases binding to desmoplakin. Fer kinase can phosphorylate tyrosine 550, which increases γ-Catenin binding to α-catenin. Thus, tyrosine phosphorylation may be important for regulation of γ-Catenin protein-protein interactions within desmosomal complexes.
Miravet, S. et al. (2003) Mol. Cell. Biol. 23(20) :7391.
McCrea, P.D. et al. (1991) Science 254:1359.
*For more information, see UniProt Accession P14923
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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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