Direct association of pp125FAK with paxillin, the focal adhesion- targeting mechanism of pp125FAK

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Direct association of pp125FAK with paxillin, the focal adhesion- targeting mechanism of pp125FAK

K Tachibana, T Sato, N D'Avirro and C Morimoto
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.

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.
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