Abstract
Interferon-alpha (IFN alpha) induces rapid tyrosine phosphorylation of the insulin receptor substrate-1 (IRS-1), a docking protein with multiple tyrosine phosphorylation sites that bind to the Src homology 2 (SH2) domains of various signaling proteins. During IFN alpha stimulation, the p85 regulatory subunit of the phosphatidylinositol 3'-kinase binds via its SH2 domains to tyrosine-phosphorylated IRS-1, and phosphatidylinositol 3'-kinase activity is detected in association with IRS-1. Thus, IFN alpha responses occur by activation of the IRS signaling system, which it shares with insulin, insulin-like growth factor-1, and interleukin-4.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Hematopoietic Stem Cells / drug effects
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Hematopoietic Stem Cells / metabolism
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Humans
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Immunoblotting
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Insulin / pharmacology
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Insulin Receptor Substrate Proteins
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Interferon-alpha / pharmacology*
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Molecular Sequence Data
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Phosphatidylinositol 3-Kinases
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Phosphoproteins / metabolism*
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Phosphorylation
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Phosphotransferases (Alcohol Group Acceptor) / genetics
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Phosphotransferases (Alcohol Group Acceptor) / metabolism*
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Precipitin Tests
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Protein Binding
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Protein-Tyrosine Kinases / metabolism
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Recombinant Fusion Proteins / metabolism
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Signal Transduction*
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Tumor Cells, Cultured
Substances
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IRS1 protein, human
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Insulin
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Insulin Receptor Substrate Proteins
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Interferon-alpha
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Peptide Fragments
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Phosphoproteins
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Recombinant Fusion Proteins
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Phosphatidylinositol 3-Kinases
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Phosphotransferases (Alcohol Group Acceptor)
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Protein-Tyrosine Kinases