p-paxillin Anticuerpo(Tyr 118): sc-14036

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The effects of some oncogenes, growth factors and neuropeptides are mediated by tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin cytoskeletal proteins. A rapid increase in tyrosine phosphorylation of paxillin, FAK and Crk-associated substrate (CAS) are prominent early events triggered by many G-protein-coupled receptors. In addition to G protein-coupled receptors, angiotensin IV (Ang IV), protein kinase C and other proteins can also mediate the tyrosine phosphorylation of paxillin. Paxillin must bind FAK for maximal phosphorylation in response to cell adhesion. FAK may function to direct tyrosine phosphorylation of paxillin in the process of transformation by the src oncogene. Tyrosine phosphorylated FAK and paxillin function to regulate the signaling mechanism of the rapid nongenomic action of dexamethasone on the Actin cytoskeleton. In glomerular epithelial cells, TNFa induces substantial reorganization of Actin cytoskeleton and focal adhesions. TNFa also simultaneoulsy mediates tyrosine phosphorylation of paxillin and FAK, which regulate Actin polymerization and the formation of focal adhesions, and may be directly involved in the redistribution of Actin.