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Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.

A search for c-Abl interacting proteins resulted in the recovery of PSTPIP1, originally identified as a binding protein of the PEST-type protein tyrosine phosphatases (PTP). PSTPIP1 was phosphorylated by c-Abl, and growth factor-induced PSTPIP1 phosphorylation was diminished in Abl null fibroblasts. PSTPIP1 was able to bridge c-Abl to the PEST-type PTPs. Several experiments suggest that the PEST-type PTPs negatively regulate c-Abl activity: c-Abl was hyperphosphorylated in PTP-PEST-deficient cells; disruption of the c-Abl-PSTPIP1-PEST-type PTP ternary complex by overexpression of PSTPIP1 mutants increased c-Abl phosphotyrosine content; and PDGF-induced c-Abl kinase activation was prolonged in PTP-PEST-deficient cells. Dephosphorylation of c-Abl by PEST-type PTP represents a novel mechanism by which c-Abl activity is regulated.

Pubmed ID: 11163214

Authors

  • Cong F
  • Spencer S
  • Côté JF
  • Wu Y
  • Tremblay ML
  • Lasky LA
  • Goff SP

Journal

Molecular cell

Publication Data

December 22, 2000

Associated Grants

  • Agency: NCI NIH HHS, Id: P01 CA75399

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • COS Cells
  • Carrier Proteins
  • Cells, Cultured
  • Cytoskeletal Proteins
  • Enzyme Activation
  • Epitopes
  • Macromolecular Substances
  • Mice
  • Mutation
  • Phosphorylation
  • Phosphotyrosine
  • Platelet-Derived Growth Factor
  • Protein Binding
  • Protein Tyrosine Phosphatase, Non-Receptor Type 12
  • Protein Tyrosine Phosphatases
  • Proto-Oncogene Proteins c-abl
  • Substrate Specificity
  • Transfection
  • Two-Hybrid System Techniques
  • Yeasts
  • src Homology Domains