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

Molecular cell | Dec 22, 2000

http://www.ncbi.nlm.nih.gov/pubmed/11163214

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 RIS Download

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

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Associated grants

  • Agency: NCI NIH HHS, Id: P01 CA75399

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