PDGF receptor activation induces p120-catenin phosphorylation at serine 879 via a PKCα-dependent pathway
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چکیده
منابع مشابه
PKCα activation of p120-catenin serine 879 phospho-switch disassembles VE-cadherin junctions and disrupts vascular integrity.
RATIONALE Adherens junctions (AJs) are the primary intercellular junctions in microvessels responsible for endothelial barrier function. Homophilic adhesion of vascular endothelial (VE) cadherin forms AJs, which are stabilized by binding of p120-catenin (p120). p120 dissociation from VE-cadherin results in loss of VE-cadherin homotypic interaction and AJ disassembly; however, the signaling mech...
متن کاملIntegrative Physiology PKC Activation of p120-Catenin Serine 879 Phospho-Switch Disassembles VE-Cadherin Junctions and Disrupts Vascular Integrity
Rationale: Adherens junctions (AJs) are the primary intercellular junctions in microvessels responsible for endothelial barrier function. Homophilic adhesion of vascular endothelial (VE) cadherin forms AJs, which are stabilized by binding of p120-catenin (p120). p120 dissociation from VE-cadherin results in loss of VE-cadherin homotypic interaction and AJ disassembly; however, the signaling mec...
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Epidermal growth factor receptor (EGFR) signals to p120(ctn) (p120), implying a role for EGFR in modulating cell-cell adhesion in epithelial tissues. p120 controls cadherin turnover, and may have other roles that modulate cadherin adhesiveness. To clarify the role for EGFR and other tyrosine kinases in regulating p120 function, we have generated and characterized a new phosphospecific antibody ...
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ژورنال
عنوان ژورنال: Experimental Cell Research
سال: 2009
ISSN: 0014-4827
DOI: 10.1016/j.yexcr.2008.09.025