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Paxillin: a focal adhesion-associated adaptor protein

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Abstract

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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Acknowledgements

Research in the author's laboratory is supported by grants from the American Cancer Society (RPG-96-021-04-CSM) and the National Institutes of Health (GM57943 and CA90901).

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  1. Department of Cell and Developmental Biology, Lineberger Comprehensive Cancer Center and Comprehensive Center for Inflammatory Disorders, University of North Carolina, Chapel Hill, NC 27599, North Carolina, USA

    Michael D Schaller

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Schaller, M. Paxillin: a focal adhesion-associated adaptor protein. Oncogene 20, 6459–6472 (2001). https://doi.org/10.1038/sj.onc.1204786

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