SH2-dependent Association of Phosphatidylinositol 3′-Kinase 85-kDa Regulatory Subunit with the Interleukin-2 Receptor β Chain

Kenneth E. Truitt, Gordon Mills, Christoph W. Turck, John B. Imboden

Research output: Contribution to journalArticle

39 Citations (Scopus)

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 - Feb 25 1994
Externally publishedYes

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Phosphatidylinositol 3-Kinase
Interleukin-2 Receptors
Tyrosine
Interleukin-2
Fusion reactions
Oligopeptides
Phosphorylation
Proteins
src Homology Domains
Immunoblotting
Immune Sera
Precipitates
Chemical activation

ASJC Scopus subject areas

  • Biochemistry

Cite this

SH2-dependent Association of Phosphatidylinositol 3′-Kinase 85-kDa Regulatory Subunit with the Interleukin-2 Receptor β Chain. / Truitt, Kenneth E.; Mills, Gordon; Turck, Christoph W.; Imboden, John B.

In: Journal of Biological Chemistry, Vol. 269, No. 8, 25.02.1994, p. 5937-5943.

Research output: Contribution to journalArticle

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AB - 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.

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