Adhesion-associated and PKC-modulated changes in serine/threonine phosphorylation of p120-catenin.

@article{Xia2003AdhesionassociatedAP,
  title={Adhesion-associated and PKC-modulated changes in serine/threonine phosphorylation of p120-catenin.},
  author={Xiaobo Xia and Debbie J. Mariner and Albert B. Reynolds},
  journal={Biochemistry},
  year={2003},
  volume={42 30},
  pages={9195-204}
}
p120-catenin (p120) was originally identified as a tyrosine kinase substrate, and subsequently shown to regulate cadherin-mediated cell-cell adhesion. Binding of the p120 Arm domain to E-cadherin appears to be necessary to maintain adequate cadherin levels for strong adhesion. In contrast, the sequence amino-terminal to the Arm domain confers a negative regulatory function that is likely to be modulated by phosphorylation. Several agents that induce rapid changes in cell-cell adhesion… CONTINUE READING
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