Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase

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作者：

B Stoyanov，S Volinia，T Hanck，I Rubio，M Loubtchenkov，D Malek，S Stoyanova，B Vanhaesebroeck，R Dhand，B Nurnberg

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摘要：

Phosphoinositide-3 kinase activity is implicated in diverse cellular responses triggered by mammalian cell surface receptors and in the regulation of protein sorting in yeast. Receptors with intrinsic and associated tyrosine kinase activity recruit heterodimeric phosphoinositide-3 kinases that consist of p110 catalytic subunits and p85 adaptor molecules containing Src homology 2 (SH2) domains. A phosphoinositide-3 kinase isotype, p110γ, was cloned and characterized. The p110γ enzyme was activated in vitro by both the α and βγ subunits of heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) and did not interact with p85. A potential pleckstrin homology domain is located near its amino terminus. The p110γ isotype may link signaling through G protein-coupled receptors to the generation of phosphoinositide second messengers phosphorylated in the D-3 position.

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关键词：

Cloning, Molecular GTP Binding Proteins Phosphotransferases Alcohol Group Acceptor 1 Phosphatidylinositol 3 Kinase Amino Acid Sequence Enzyme Activation Guanosine 5 O 3 Thiotriphosphate Hydrogen Ion Concentration Molecular Sequence Data Phosphatidylinositols