Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain
UMass Chan Affiliations
Program in Molecular Medicine and Department of Biochemistry and Molecular BiologyDocument Type
Journal ArticlePublication Date
1996-06-07Keywords
1-Phosphatidylinositol 3-Kinase3T3 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
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
J Biol Chem. 1996 Jun 7;271(23):13304-7.
DOI
10.1074/jbc.271.23.13304Permanent Link to this Item
http://hdl.handle.net/20.500.14038/42449PubMed ID
8663140Related Resources
ae974a485f413a2113503eed53cd6c53
10.1074/jbc.271.23.13304