ABSTRACT
Cells communicate with their extracellular environment via a variety of cellular receptors. Cytoskeletal proteins that become phosphorylated include the focal adhesion kinase (FAK), p130cas, and paxillin. Paxillin co-localizes with FAK and vinculin, along with several other structural and regulatory proteins, to points of contact of the cell membrane with the ECM, termed focal adhesions. As a cytoskeletal adaptor protein, paxillin is a biochemical-structural composite of protein recognition domains. The primary amino acid sequence of paxillin reveals a diversity of protein-protein interaction motifs, as well as the presence of multiple sites that may serve as targets of protein phosphorylation. Paxillin, a focal adhesion-related adaptor protein is found localized to focal adhesions in adherent cells.
