Fig. 7. SETA promotes the association between AIP1 and PYK-2. AIP1 and AIP1 mutants were transiently co-transfected into HEK293 cells with SETA or lacZ control plasmid. Endogenous FAK or PYK-2 was immunoprecipitated and the pellet subsequently analyzed by immunoblotting for AIP1 and SETA. When compared with wild-type AIP1, all mutants were significantly reduced in their ability to bind FAK and PYK-2, with the AIP1Y319F mutant, which is altered at a potential src phosphorylation site, showing no detectable binding to either focal adhesion kinase. The PxxP-deficient mutants were also negatively impacted in their binding capacity but remained detectable in the complex. Co-transfection of SETA enhanced wild-type AIP1 binding to PYK-2 but not to FAK. Furthermore, SETA was able to partially restore the binding of AIP1 and the two AIP1 deletion mutants to FAK/PYK-2.