| First Author | Virbasius JV | Year | 1996 |
| Journal | J Biol Chem | Volume | 271 |
| Issue | 23 | Pages | 13304-7 |
| PubMed ID | 8663140 | Mgi Jnum | J:33394 |
| Mgi Id | MGI:80875 | Doi | 10.1074/jbc.271.23.13304 |
| Citation | Virbasius JV, et al. (1996) Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain. J Biol Chem 271(23):13304-7 |
| abstractText | 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. |
