Paxillin (Ser-83), phospho-specific Antibody

Paxillin, a focal adhesion protein, is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and SH3-/SH2-binding domains that participate in a variety of protein-protein interactions with kinases, GTPase-activating proteins, and cytoskeletal proteins. Phosphorylation of paxillin occurs at both tyrosine and serine sites. Serine phosphorylation of paxillin occurs in response to growth-factor activation and fibronectins. Both ERK and p38MAPK kinases phosphorylate serine 83 in vitro. HGF stimulation of murine epithelial cells leads to ERK-mediated phosphorylation of Ser-83, which is required for HGF-induced cell spreading and migration. In addition, Ser-83 is phosphorylated in response to NGF in PC12 cells, and this phosphorylation may be involved in neurite extension. In human paxillin, Ser-85 rather than Ser-83 may be the site phosphorylated by p38 MAPK and mutation of this site inhibits NGF-induced neurite extension. Thus, serine residues in the N-terminal region of paxillin may be important for growth-factor mediated changes in activity.

References

*For more information, see UniProt Accession Q8VI36

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