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Y-27632, an Inhibitor of Rho-Associated Kinases, Prevents Tyrosine Phosphorylation of Focal Adhesion Kinase and Paxillin Induced by Bombesin: Dissociation from Tyrosine Phosphorylation of p130cas

✍ Scribed by James Sinnett-Smith; J.Adrian Lunn; Daniela Leopoldt; Enrique Rozengurt


Book ID
115604004
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
370 KB
Volume
266
Category
Article
ISSN
0014-4827

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Dissociation of focal adhesion kinase an
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## Abstract Tyrosine phosphorylation of the nonreceptor tyrosine kinase p125 focal adhesion kinase (FAK) and the adapter protein paxillin is rapidly increased by multiple agonists, including bombesin (BOM) and lysophosphatidic acid (LPA), through heptahelical G protein‐coupled receptors (GPCRs). Th

Tyrosine phosphorylation of p125fak, p13
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The experiments presented here were designed to examine the contribution of the extracellular signal-regulated mitogen-activated protein kinases (ERKs) to the tyrosine phosphorylation of the focal adhesion proteins p125 Fak , p130 Cas , and paxillin induced by G protein-coupled receptors (GPCRs) and