A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits

L. Stephens, A. Smrcka, F. T. Cooke, T. R. Jackson, P. C. Sternweis, P. T. Hawkins

Research output: Contribution to journalArticle

504 Scopus citations

Abstract

Phosphoinositide 3 kinase (PI3K) is a key signaling enzyme implicated in receptor-stimulated mitogenesis, oxidative bursting in neutrophils, membrane ruffling, and glucose uptake. A PI3K has already been purified, cloned, and shown to be regulated by receptors that act via tyrosine kinase-dependent regulatory mechanisms. We report that an immunologically, pharmacologically, and chromatographically distinct form of PI3K activity present in neutrophils and U937 cells is specifically activated by G protein βγ subunits. This data suggests PI3Ks conform to the paradigm set by receptor regulation of phosphoinositidase Cs: different receptor transduction systems specifically regulate dedicated isoforms of effector protein.

Original languageEnglish (US)
Pages (from-to)83-93
Number of pages11
JournalCell
Volume77
Issue number1
DOIs
StatePublished - Apr 8 1994

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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