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http://en.wikipedia.org/wiki/Paxillin Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge[1] and should not be confused with the neurotoxin paxilline. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal region of paxillin is rich in protein-protein interaction sites. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT. Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk ²»ÖªµÀÄã×îºóÒ»¸ö´ÊÊÇ·ñ´ò´íÁË¡£ |
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