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

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.

Pubmed ID: 10625692

Authors

  • Shen Y
  • Lyons P
  • Cooley M
  • Davidson D
  • Veillette A
  • Salgia R
  • Griffin JD
  • Schaller MD

Journal

The Journal of biological chemistry

Publication Data

January 14, 2000

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM53666
  • Agency: NIGMS NIH HHS, Id: GM57943

Mesh Terms

  • Animals
  • Binding Sites
  • Cell Line
  • Cells, Cultured
  • Chick Embryo
  • Cytoskeletal Proteins
  • Glutathione Transferase
  • Humans
  • Paxillin
  • Phosphoproteins
  • Protein Tyrosine Phosphatase, Non-Receptor Type 12
  • Protein Tyrosine Phosphatases
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Substrate Specificity
  • Transfection