Journal
ONCOGENE
Volume 20, Issue 44, Pages 6459-6472Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.onc.1204786
Keywords
paxillin; integrin signaling; phosphotyrosine; cytoskeleton; cell motility; FAK
Funding
- NCI NIH HHS [CA90901] Funding Source: Medline
- NIGMS NIH HHS [GM57943] Funding Source: Medline
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Paxillin 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.
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