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

doi:10.1016/0092-8674(94)90237-2

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

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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 language	English (US)
Pages (from-to)	83-93
Number of pages	11
Journal	Cell
Volume	77
Issue number	1
DOIs	https://doi.org/10.1016/0092-8674(94)90237-2
State	Published - Apr 8 1994

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/0092-8674(94)90237-2

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

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.",

author = "L. Stephens and A. Smrcka and Cooke, {F. T.} and Jackson, {T. R.} and Sternweis, {P. C.} and Hawkins, {P. T.}",

note = "Funding Information: The monoclonal antibodies used in this work were generously provided by I. Gout and Professor M. Waterfield, Fellows of the Royal Society (FRS), of the Ludwig Institute. Useful discussions with Dr. M. Thelen, Dr. M. Wymann, Dr. J. Hepier, and Dr. R. F. Iffine, FRS, are also acknowledged. P. T. H. is an Agricultural and Food Research Council postdoctoral Fellow. This work was funded by a North Atlantic Treaty Organization travel grant, the Leukemia Research Fund, and a collabo rative research award from Amersham International.",

year = "1994",

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doi = "10.1016/0092-8674(94)90237-2",

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AU - Stephens, L.

AU - Smrcka, A.

AU - Cooke, F. T.

AU - Jackson, T. R.

AU - Sternweis, P. C.

AU - Hawkins, P. T.

N1 - Funding Information: The monoclonal antibodies used in this work were generously provided by I. Gout and Professor M. Waterfield, Fellows of the Royal Society (FRS), of the Ludwig Institute. Useful discussions with Dr. M. Thelen, Dr. M. Wymann, Dr. J. Hepier, and Dr. R. F. Iffine, FRS, are also acknowledged. P. T. H. is an Agricultural and Food Research Council postdoctoral Fellow. This work was funded by a North Atlantic Treaty Organization travel grant, the Leukemia Research Fund, and a collabo rative research award from Amersham International.

PY - 1994/4/8

Y1 - 1994/4/8

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AB - 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.

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

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ASJC Scopus subject areas

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