Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3'-kinase.
作者： U. Dechert , K.B. Leslie , J.W. Schrader , F. Jirik , M.J. Welham
DOI: 10.1016/S0021-9258(17)31581-8
关键词:
摘要: Binding of interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor (GM-CSF) to their high affinity cell surface receptors induces tyrosine phosphorylation a similar set protein substrates. We have identified one these common substrates (p70) as the protein-tyrosine phosphatase SHPTP2. The Src homology 2 (SH2) domain adaptor Grb2 bound with tyrosine-phosphorylated SHPTP2 following treatment cells IL-3 or GM-CSF, but not IL-4. This interaction was inhibited by two phosphotyrosine peptides, based on sequences within SHPTP2, which conform postulated consensus sequence for SH2 recognition. Following IL-4, co-immunoprecipitated antibodies directed against p85 subunit PI 3‘-kinase. partially blocked same phosphopeptides that Grb2-SH2 binding Importantly, resulted in 2-3-fold increase activity. These results suggest may play an important role integrating signals from GM-CSF both Ras
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