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 tyrosine, threonine, and serine sites. Serine and threonine phosphorylation of paxillin occur in response to growth-factor activation, PKC activators, and fibronectins. Phosphorylation of Ser-85, Ser-178, and Thr-538 may be important sites for regulating paxillin activity. Paxillin phosphorylation of Thr-538 occurs in response to TPA-activated PKCs in vitro, and this phosphorylation may contribute to dissolution of the actin cytoskeleton and redistribution of LFA-1 integrins in vivo.
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Woodrow, M.A. (2003) Exp. Cell. Res. 287(2):325-338.
*For more information, see UniProt Accession P49023
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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.
Product References:Wu, D. W. et al. (2014) Oncogene 33(35): 4385. (WB: CCM3 cells)
This kit contains: