2003
cAMP promotes pancreatic β-cell survival via CREB-mediated induction of IRS2
Jhala U, Canettieri G, Screaton R, Kulkarni R, Krajewski S, Reed J, Walker J, Lin X, White M, Montminy M. cAMP promotes pancreatic β-cell survival via CREB-mediated induction of IRS2. Genes & Development 2003, 17: 1575-1580. PMID: 12842910, PMCID: PMC196130, DOI: 10.1101/gad.1097103.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell LineCell SurvivalColforsinCyclic AMPCyclic AMP Response Element-Binding ProteinDiabetes MellitusGene Expression RegulationGlucagonGlucagon-Like Peptide 1GlucoseGlucose IntoleranceHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsIslets of LangerhansMiceMice, TransgenicPeptide FragmentsPhosphoproteinsPhosphorylationPromoter Regions, GeneticProtein PrecursorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionTransfectionTransgenesTumor Cells, CulturedConceptsPancreatic β-cell survivalActivity of CREBSecond messenger cAMPSurvival kinase AktΒ-cell survivalKinase AktPathway componentsA-CREBCREB actionExpression of IRS2Cell survivalBeta-cell apoptosisDirect targetIslet cell survivalNovel mechanismCREBIRS2ExpressionCAMPInductionTransgeneAktIGF-1ApoptosisSurvival
1999
Insulin action and type 2 diabetes: lessons from knockout mice
Withers D, White M. Insulin action and type 2 diabetes: lessons from knockout mice. Current Opinion In Endocrinology Diabetes And Obesity 1999, 6: 141-145. DOI: 10.1097/00060793-199904000-00010.Peer-Reviewed Original ResearchBeta-cell functionType 2 diabetesInsulin signal transduction pathwayInsulin receptor resultsSignal transduction pathwaysGlucose homeostasisInsulin receptor substrateClassical insulin target tissuesInsulin actionBeta cell-specific deletionCell functionPancreatic beta-cell functionPeripheral insulin actionKnockout mouse modelInsulin target tissuesCell-specific deletionTransduction pathwaysReceptor substrateSignaling pathwaysUnsuspected roleNew experimental modelInsulin resistanceNovel insightsNovel mechanismGlucose disposal
1997
Calmodulin Activates Phosphatidylinositol 3-Kinase*
Joyal J, Burks D, Pons S, Matter W, Vlahos C, White M, Sacks D. Calmodulin Activates Phosphatidylinositol 3-Kinase*. Journal Of Biological Chemistry 1997, 272: 28183-28186. PMID: 9353264, DOI: 10.1074/jbc.272.45.28183.Peer-Reviewed Original ResearchConceptsSrc homology 2 domainIntact cellsPhosphorylation of phosphatidylinositolActivates PhosphatidylinositolVesicular traffickingEukaryotic cellsEffector proteinsRegulatory subunitCytoskeletal organizationUbiquitous Ca2PhosphatidylinositolIntracellular eventsNovel mechanismAffinity chromatographyGrowth factorCalmodulinCalmodulin antagonistsMultiple processesCellsCoimmunoprecipitationDirect linkPhosphorylationTraffickingSubunitsCa2Tyr624 and Tyr628 in Insulin Receptor Substrate-2 Mediate Its Association with the Insulin Receptor*
Sawka-Verhelle D, Baron V, Mothe I, Filloux C, White M, Van Obberghen E. Tyr624 and Tyr628 in Insulin Receptor Substrate-2 Mediate Its Association with the Insulin Receptor*. Journal Of Biological Chemistry 1997, 272: 16414-16420. PMID: 9195949, DOI: 10.1074/jbc.272.26.16414.Peer-Reviewed Original ResearchConceptsInsulin receptorIRS-2Tyrosine residuesPleckstrin homology domainPeptide competition studiesInsulin receptor substrateAmino acids 591Homology domainReceptor substrateBinding domainsRegulatory loopIRS-1Novel mechanismPosition 624ResiduesCompetition studiesReceptorsDomainIts AssociationPhosphotyrosinePhosphorylationBindsBindingRegionInteraction