SH2-dependent association of phosphatidylinositol 3'-kinase 85-kDa regulatory subunit with the interleukin-2 receptor β chain

K. E. Truitt, G. B. Mills, C. W. Turck, J. B. Imboden

    Research output: Contribution to journalArticle

    40 Scopus citations

    Abstract

    Interleukin-2 (IL-2) signaling results in tyrosine phosphorylation of the 75-kDa IL-2 receptor (IL-2R) β chain and the activation of phosphatidylinositol 3'-kinase (PI3-K). Herein, we demonstrate that the 85- kDa (p85) regulatory subunit of PI3-K physically associates with the tyrosine-phosphorylated IL-2R β chain. A fusion protein containing both the amino- and the carboxyl-terminal src homology 2 domains of p85 precipitates an 80-kDa tyrosine-phosphorylated protein (pp80) from the lysates of IL-2- stimulated, but not unstimulated, human T lymphoblasts. Preclearing studies and immunoblotting with an antiserum to the IL-2R β chain demonstrates that pp80 represents a portion of the IL-2R β chain pool. A tyrosine- phosphorylated oligopeptide corresponding to tyrosine 392 of the IL-2R β chain partially inhibits binding of the IL-2R β chain by p85 fusion protein, raising the possibility that this residue plays a role in the interaction of PI3-K with the receptor.

    Original languageEnglish (US)
    Pages (from-to)5937-5943
    Number of pages7
    JournalJournal of Biological Chemistry
    Volume269
    Issue number8
    StatePublished - Jan 1 1994

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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