Plakoglobin, JUP, Desmoplakin III, Desmoplakin-3, catenin gamma1
Plakoglobin (gamma-Catenin) is a catenin family member identified as a component of desmosomes. gamma-Catenin has high homology to beta-catenin and, like beta-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. One molecule of alpha-catenin and at least one molecule of beta-catenin and gamma-Catenin simultaneously bind to a single cadherin molecule. A 19-amino acid sequence of desmoglein was found to be critical for binding of gamma-Catenin. Similar catenin-binding domains found in cadherins, suggest a common mechanism for gamma-Catenin localization to both adherens junctions and desmosomes. Phosphorylation of tyrosine residues in gamma-Catenin can modify its interactions with other proteins. Phosphorylation of tyrosine 644 decreases gamma-Catenin association with alpha-catenin, but increases binding to desmoplakin. Fer kinase can phosphorylate tyrosine 550, which increases gamma-Catenin binding to alpha-catenin. Thus, tyrosine phosphorylation may be important for regulation of gamma-Catenin protein-protein interactions within desmosomal complexes.
Plakoglobin (gamma-Catenin) is a catenin family member identified as a component of desmosomes. gamma-Catenin has high homology to beta-catenin and, like beta-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. One molecule of alpha-c
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