The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo

Yu Shen, Patrick Lyonst, Marion Cooley, Dominique Davidson, André Veillette, Ravi Salgiall, James D. Griffin, Michael D. Schaller

Research output: Contribution to journalArticle

58 Scopus citations

Abstract

The noncatalytic domain of protein-tyrosine phosphatase (PTP)-PEST contains a binding site for the focal adhesion-associated protein paxillin. This binding site has been narrowed to a 52-residue sequence that is composed of two nonoverlapping, weak paxillin binding sites. The PTP-PEST binding site on paxillin has been mapped to the two carboxyl-terminal LIM (lin11, isl-1, and mec-3) domains. Transient expression of PTP-PEST reduced tyrosine phosphorylation of p130(cas), as anticipated. A PTP-PEST mutant defective for binding p130(cas) does not cause a reduction in its tyrosine phosphorylation in vivo. Expression of PTP-PEST also caused a reduction of phosphotyrosine on paxillin. Expression of mutants of PTP-PEST with deletions in the paxillin- binding site did not associate with paxillin in vivo and failed to cause a reduction in the phosphotyrosine content of paxillin. These results demonstrate that paxillin can serve as a PTP-PEST substrate in vivo and support the model that a noncatalytic domain interaction recruits paxillin to PTP-PEST to facilitate its dephosphorylation.

Original languageEnglish (US)
Pages (from-to)1405-1413
Number of pages9
JournalJournal of Biological Chemistry
Volume275
Issue number2
DOIs
StatePublished - Jan 14 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Shen, Y., Lyonst, P., Cooley, M., Davidson, D., Veillette, A., Salgiall, R., Griffin, J. D., & Schaller, M. D. (2000). The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo. Journal of Biological Chemistry, 275(2), 1405-1413. https://doi.org/10.1074/jbc.275.2.1405