Focal adhesion kinase (pp125FAK) is localized to focal adhesions and tyrosine phosphorylated by the engagement of beta 1 integrins. However, it is unclear how pp125FAK is linked to integrin molecules. We demonstrate that pp125FAK is directly associated with paxillin, a 68-kD cytoskeleton protein. The COOH-terminal domain of pp125FAK spanning FAK residues 919-1042 is sufficient for paxillin binding and has vinculin-homologous amino acids, which are essential for paxillin binding. Microinjection and subsequent immunohistochemical analysis reveal that glutathione S-transferase-FAK fusion proteins, which bind to paxillin, localize to focal adhesions, whereas fusion proteins with no paxillin-binding activity do not localize to focal adhesions. These findings strongly suggest that pp125FAK is localized to focal adhesions by the direct association with paxillin.
Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK.
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K Tachibana, T Sato, N D'Avirro, C Morimoto; Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK.. J Exp Med 1 October 1995; 182 (4): 1089–1099. doi: https://doi.org/10.1084/jem.182.4.1089
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