Interferon-α engages the insulin receptor substrate-1 to associate with the phosphatidylinositol 3'-kinase

Shahab Uddin, Lynne Yenush, Xiao Jian Sun, Michelle E. Sweet, Morris F. White, Leonidas C. Platanias*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

184 Scopus citations

Abstract

Interferon-α (IFNα) 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 IFNα 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, IFNα responses occur by activation of the IRS signaling system, which it shares with insulin, insulin-like growth factor-1, and interleukin-4.

Original languageEnglish (US)
Pages (from-to)15938-15941
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number27
DOIs
StatePublished - 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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