Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase
✍ Scribed by Wade, Ramon; Bohl, Joanna; Vande Pol, Scott
- Book ID
- 110066240
- Publisher
- Nature Publishing Group
- Year
- 2002
- Tongue
- English
- Weight
- 393 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0950-9232
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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
## Abstract Treatment of intact Swiss 3T3 cells with calyculin‐A, an inhibitor of myosin light chain (MLC) phosphatase, induces tyrosine phosphorylation of p125^Fak^ in a sharply concentration‐ and time‐dependent manner. Maximal stimulation was 4.2 ± 2.1‐fold (n = 14). The stimulatory effect of cal