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.
Ishibe, S. et al. (2004) Mol. Cell 16 :257-267.
*For more information, see UniProt Accession Q8VI36
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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