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. Author manuscript; available in PMC: 2008 Aug 1.
Published in final edited form as: Cell Signal. 2007 Mar 30;19(8):1733–1744. doi: 10.1016/j.cellsig.2007.03.010

Figure 5.

Figure 5

Paxillin binding to GIT1 FAH domain mutants.

A. Point mutants within the GIT1 carboxyl terminal four-helix bundle identify the paxillin site as the helix 1/4 interface. The indicated GIT1/Flag mutants were transfected into COS7 cells. Cells were scraped and lysed after 48 hours, and soluble lysates immunoprecipitated by addition of M2 Flag-agarose beads. Co-immunoprecipitated endogenous paxillin and β–PIX were measured by immunoblotting with specific antisera, and precipitated GIT1/Flag directly visualized with M2 Flag-HRP conjugate.

B. Mutational analysis mapped onto the surface of the GIT1 model. Mutated residues shown in Figure 1A and analyzed in Figure 3B (and Figure 7 and Figure 9) are colored according to their effect on paxillin binding: red: reduced LD4 binding, green: no influence on LD4 binding, blue: enhanced LD4 binding, grey: not mutated. Together, these data suggest that GIT1 binds LD4 between helices 1 and 4, but not helices 2 and 3.