Title

Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain

UMMS Affiliation

Program in Molecular Medicine and Department of Biochemistry and Molecular Biology

Publication Date

1996-06-07

Document Type

Article

Subjects

1-Phosphatidylinositol 3-Kinase; 3T3 Cells; Amino Acid Sequence; Androstadienes; Animals; Base Sequence; Cloning, Molecular; DNA Primers; DNA, Complementary; Drosophila; Enzyme Inhibitors; Humans; Mice; Molecular Sequence Data; Molecular Structure; Phosphotransferases (Alcohol Group; Acceptor); Sequence Homology, Amino Acid; Substrate Specificity

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Phosphatidylinositol (PI) 3-kinases catalyze the formation of 3'-phosphoinositides, which appear to promote cellular responses to growth factors and such membrane trafficking events as insulin-stimulated translocation of intracellular glucose transporters. We report here the cloning of a novel PI 3-kinase, p170, from cDNA of insulin-sensitive mouse 3T3-L1 adipocytes. Mouse p170 utilizes PI and to a limited extent PI 4-P as substrates, in contrast to the PI-specific yeast VPS34 homolog PtdIns 3-kinase and the p110 PI 3-kinases, which phosphorylate PI, PI 4-P, and PI 4,5-P2. Mouse p170 is also distinct from PtdIns 3-kinase or the p110 PI 3-kinases in exhibiting a 10-fold lower sensitivity to wortmannin. Unique structural elements of p170 include C-terminal sequences strikingly similar to the phosphoinositide-binding C2 domain of protein kinase C isoforms, synaptotagmins, and other proteins. These features of mouse p170 are shared with a recently cloned Drosophila PI 3-kinase, DmPI3K_68D. Together, these proteins define a new class of PI 3-kinase likely influenced by cellular regulators distinct from those acting upon p110- or VPS34-like PI 3-kinases.

DOI of Published Version

10.1074/jbc.271.23.13304

Source

J Biol Chem. 1996 Jun 7;271(23):13304-7.

Journal/Book/Conference Title

The Journal of biological chemistry

Related Resources

Link to Article in PubMed

PubMed ID

8663140

Link to Full Text

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