Interleukin-3 Induces the Association of the Inositol 5-Phosphatase SHIP with SHP2
| Autor: | Jacqueline E. Damen, Ling Liu, Mark D. Ware, Gerald Krystal |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
SH2 Domain-Containing Protein Tyrosine Phosphatases
Protein Tyrosine Phosphatase Non-Receptor Type 11 Protein tyrosine phosphatase Biology SH2 domain Biochemistry src Homology Domains Mice Animals Tyrosine Molecular Biology Peptide sequence Cells Cultured chemistry.chemical_classification Binding Sites Protein Tyrosine Phosphatase Non-Receptor Type 6 Intracellular Signaling Peptides and Proteins technology industry and agriculture Cell Biology Precipitin Tests Phosphoric Monoester Hydrolases Enzyme chemistry Phosphatidylinositol-3 4 5-Trisphosphate 5-Phosphatases Phosphorylation Interleukin-3 Protein Tyrosine Phosphatases Signal transduction Intracellular Protein Binding Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 272:10998-11001 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.17.10998 |
| Popis: | We recently purified and cloned a 145-kDa protein that becomes tyrosine phosphorylated and associated with Shc in response to multiple cytokines. Based on its predicated amino acid sequence and its enzymatic activity, we have called this protein SHIP, for Src homology 2-containing inositol phosphatase. To gain further insight into the intracellular pathways that this putative signal transduction intermediate might regulate we have investigated whether SHIP binds to intracellular proteins other than Shc. The results presented herein demonstrate that following interleukin-3 stimulation, SHIP binds to the tyrosine phosphatase, SHP2 (also called Syp, PTP1D, SHPTP2, and PTP2C) and that Shc is not present in these SHIP-SHP2 complexes. Time course studies reveal that SHIP's association with SHP2 is transient and is maximal at 10 min of stimulation with interleukin-3. We further show that the association of SHIP with SHP2 occurs through the direct interaction of the SH2 domain of SHIP with a pYXN(I/V) sequence within SHP2. |
| Databáze: | OpenAIRE |
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