Show simple item record

dc.contributor.authorVirbasius, Joseph V.
dc.contributor.authorGuilherme, Adilson L.
dc.contributor.authorCzech, Michael P.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:13Z
dc.date.available2022-08-23T16:54:13Z
dc.date.issued1996-06-07
dc.date.submitted2008-08-15
dc.identifier.citation<p>J Biol Chem. 1996 Jun 7;271(23):13304-7.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.271.23.13304
dc.identifier.pmid8663140
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42449
dc.description.abstractPhosphatidylinositol (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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8663140&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.271.23.13304
dc.subject1-Phosphatidylinositol 3-Kinase
dc.subject3T3 Cells
dc.subjectAmino Acid Sequence
dc.subjectAndrostadienes
dc.subjectAnimals
dc.subjectBase Sequence
dc.subjectCloning, Molecular
dc.subjectDNA Primers
dc.subjectDNA, Complementary
dc.subjectDrosophila
dc.subjectEnzyme Inhibitors
dc.subjectHumans
dc.subjectMice
dc.subjectMolecular Sequence Data
dc.subjectMolecular Structure
dc.subjectPhosphotransferases (Alcohol Group
dc.subjectAcceptor)
dc.subjectSequence Homology, Amino Acid
dc.subjectSubstrate Specificity
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume271
dc.source.issue23
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/798
dc.identifier.contextkey579683
html.description.abstract<p>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.</p>
dc.identifier.submissionpathoapubs/798
dc.contributor.departmentProgram in Molecular Medicine and Department of Biochemistry and Molecular Biology
dc.source.pages13304-7


This item appears in the following Collection(s)

Show simple item record