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Direct Association of Protein-tyrosine Phosphatase PTP-PEST with Paxillin
Journal article   Open access   Peer reviewed

Direct Association of Protein-tyrosine Phosphatase PTP-PEST with Paxillin

Yu Shen, Galen Schneider, Jean-François Cloutier, André Veillette and Michael D Schaller
The Journal of biological chemistry, Vol.273(11), pp.6474-6481
03/1998
DOI: 10.1074/jbc.273.11.6474
PMID: 9497381
url
https://doi.org/10.1074/jbc.273.11.6474View
Published (Version of record) Open Access

Abstract

Tyrosine phosphorylation of focal adhesion-associated proteins may be involved in the regulation of the cytoskeleton and in the control of signals for growth and survival. The focal adhesion kinase (FAK) functions in regulating tyrosine phosphorylation of several of these proteins, including paxillin, tensin, and p130(cas). Protein- tyrosine phosphatases, the counterparts of protein-tyrosine kinases, also presumably regulate phosphorylation of these proteins. We have tested the hypothesis that FAK intimately associates with a protein-tyrosine phosphatase. Protein-tyrosine phosphatase activity associated with the recombinant C-terminal domain of FAK in vitro and could be coimmunoprecipitated with both FAK and paxillin from lysates of chicken embryo cells. However, the interaction with FAK appeared to be indirect and mediated via paxillin. The protein-tyrosine phosphatase was subsequently identified as protein-tyrosine phosphatase-PEST, a nonreceptor protein-tyrosine phosphatase. The C-terminal noncatalytic domain of protein-tyrosine phosphatase-PEST directly bound to paxillin in vitro. The association of both a protein-tyrosine kinase and a protein-tyrosine phosphatase with paxillin suggests that paxillin may play a critical role in the regulation of the phosphotyrosine content of proteins in focal adhesions.

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