1999
Endothelin-1 modulates insulin signaling through phosphatidylinositol 3-kinase pathway in vascular smooth muscle cells.
Jiang Z, Zhou Q, Chatterjee A, Feener E, Myers M, White M, King G. Endothelin-1 modulates insulin signaling through phosphatidylinositol 3-kinase pathway in vascular smooth muscle cells. Diabetes 1999, 48: 1120-1130. PMID: 10331419, DOI: 10.2337/diabetes.48.5.1120.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEndothelin Receptor AntagonistsEndothelin-1Enzyme InhibitorsGTP-Binding ProteinsHumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMaleMuscle, Smooth, VascularPeptides, CyclicPertussis ToxinPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsPhosphoserineProtein Kinase CRatsRats, ZuckerSignal TransductionTetradecanoylphorbol AcetateVirulence Factors, BordetellaConceptsInsulin-stimulated phosphatidylinositolProtein kinase CIRS-2P85 subunitSerine phosphorylationSmooth muscle cellsInsulin receptor beta subunitInsulin-induced phosphatidylinositolInsulin receptor substrateReceptor beta subunitMuscle cellsTreatment of cellsArterial smooth muscle cellsReceptor substratePretreatment of cellsVascular smooth muscle cellsBeta subunitKinase CPhosphatidylinositolIndependent pathwaysSpecific inhibitorET-1SubunitsPhosphorylationPathway
1998
Interaction of insulin receptor substrate-1 (IRS-1) with phosphatidylinositol 3-kinase: effect of substitution of serine for alanine in potential IRS-1 serine phosphorylation sites.
Delahaye L, Mothe-Satney I, Myers M, White M, Van Obberghen E. Interaction of insulin receptor substrate-1 (IRS-1) with phosphatidylinositol 3-kinase: effect of substitution of serine for alanine in potential IRS-1 serine phosphorylation sites. Endocrinology 1998, 139: 4911-9. PMID: 9832428, DOI: 10.1210/endo.139.12.6379.Peer-Reviewed Original ResearchConceptsInsulin receptor substrate-1Protein kinase B activitySerine phosphorylation sitesRegulatory subunitReceptor substrate-1Phosphorylation sitesPotential binding sitesTyrosine phosphorylationSubstrate-1Potential tyrosine phosphorylation sitesIRS-1 interactsPotential serine phosphorylation sitesWild-type IRS-1Two-hybrid systemTyrosine phosphorylation sitesInsulin-stimulated phosphatidylinositolPhosphorylate IRS-1P85alpha regulatory subunitBinding sitesYeast kinasesThreonine phosphorylationSerine mutantsYXXM motifsB activityP85alpha
1993
Insulin-Stimulated Oocyte Maturation Requires Insulin Receptor Substrate 1 and Interaction with the SH2 Domains of Phosphatidylinositol 3-Kinase
Chuang L, Myers M, Backer J, Shoelson S, White M, Birnbaum M, Kahin C. Insulin-Stimulated Oocyte Maturation Requires Insulin Receptor Substrate 1 and Interaction with the SH2 Domains of Phosphatidylinositol 3-Kinase. Molecular And Cellular Biology 1993, 13: 6653-6660. DOI: 10.1128/mcb.13.11.6653-6660.1993.Peer-Reviewed Original ResearchSrc homology 2 domainSrc homology 2PtdIns 3-kinaseSrc homology 2 domains of p85Glutathione S-transferase fusion proteinS-transferase fusion proteinDomains of p85IRS-1Ras-GAPP85 subunit of PtdIns 3-kinaseFusion proteinActivation of PtdIns 3-kinasePtdIns 3-kinase activitySubstrate 1Phosphorylation of IRS-1IRS-1 associationInsulin receptor substrate 1Insulin-stimulated phosphatidylinositolIRS-1 proteinPhosphorylated IRS-1Progesterone-induced oocyte maturationP85 subunitOocyte maturationInsulin signalingResponse to hormonal stimulation