Paxillin is involved in the integration of growth factor- and adhesion-mediated signal transduction pathways at focal adhesion sites. The LD motif of paxillin has been implicated in its binding to FAK, vinculin, and paxillin-kinase linker (p95PKL). p95PKL couples paxillin to a protein complex containing p21 GTPase-activated kinase (PAK), Nck, and the guanine nucleotide exchange factor, PIX. The sequence of p95PKL, highly homologous to human GIT1 and GIT2, predicts a structure that contains an N-terminal ARF-GAP domain containing a Zn2+ finger, three ankyrin repeats, an EF hand domain, and two IQ motifs. p95PKL binds to both paxillin and PIX and colocalizes with paxillin at focal adhesion sites. Overexpression of a paxillin LD4 deletion mutant in neuroblastoma cells inhibits insulin-like growth factor-1 mediated lamellipodia formation. Microinjection of this mutant into NIH3T3 cells has been reported to decrease migration into a wound. These alterations in cell motility are thought to involve PAK-mediated regulation of the actin cytoskeleton, since the LD4 motif of paxillin is required for p95PKL-dependent recruitment of PAK/PIX complexes to paxillin-containing focal adhesions sites. This antibody has been reported to recognize GIT1 and GIT2 proteins.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.