Paxillin

Paxillin is a is_associated_with::signal transduction is_associated_with::adaptor protein discovered in 1990 in the laboratory of is_associated_with::Keith Burridge. The C-terminal region of paxillin contains four is_associated_with::LIM domains that target paxillin to is_associated_with::focal adhesions. It is presumed through a direct association with the cytoplasmic tail of beta-is_associated_with::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 focal adhesion kinase (FAK), structural proteins, such as is_associated_with::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.