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Paxillin: a focal adhesion-associated adaptor protein Schaller MDOncogene 2001[Oct]; 20 (44): 6459-72Paxillin is a focal adhesion-associated, phosphotyrosine-containing protein that may play a role in several signaling pathways. Paxillin contains a number of motifs that mediate protein-protein interactions, including LD motifs, LIM domains, an SH3 domain-binding site and SH2 domain-binding sites. These motifs serve as docking sites for cytoskeletal proteins, tyrosine kinases, serine/threonine kinases, GTPase activating proteins and other adaptor proteins that recruit additional enzymes into complex with paxillin. Thus paxillin itself serves as a docking protein to recruit signaling molecules to a specific cellular compartment, the focal adhesions, and/or to recruit specific combinations of signaling molecules into a complex to coordinate downstream signaling. The biological function of paxillin coordinated signaling is likely to regulate cell spreading and motility.|Amino Acid Motifs[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Cell Adhesion[MESH]|Cell Movement[MESH]|Cell Nucleus/metabolism[MESH]|Cytoskeletal Proteins/*chemistry/*metabolism/*physiology[MESH]|Humans[MESH]|Molecular Sequence Data[MESH]|Paxillin[MESH]|Phosphoproteins/*chemistry/*metabolism/*physiology[MESH]|Phosphorylation[MESH]|Protein Binding[MESH]|Protein Structure, Tertiary[MESH]|Sequence Homology, Amino Acid[MESH]|Signal Transduction[MESH]|src Homology Domains[MESH] |
