2004
Disruption of the SH2-B Gene Causes Age-Dependent Insulin Resistance and Glucose Intolerance
Duan C, Yang H, White M, Rui L. Disruption of the SH2-B Gene Causes Age-Dependent Insulin Resistance and Glucose Intolerance. Molecular And Cellular Biology 2004, 24: 7435-7443. PMID: 15314154, PMCID: PMC506995, DOI: 10.1128/mcb.24.17.7435-7443.2004.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdipose TissueAgingAnimalsBlood GlucoseCarrier ProteinsCell LineDietary FatsGlucose IntoleranceHomeostasisHumansInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIntracellular Signaling Peptides and ProteinsIslets of LangerhansLiverMaleMiceMice, Inbred StrainsMice, KnockoutMitogen-Activated Protein KinasesMuscle, SkeletalPhosphatidylinositol 3-KinasesPhosphoproteinsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptor, InsulinSignal TransductionConceptsSrc homology 2Insulin receptor substrate-1Insulin receptor activationInsulin receptorTyrosine phosphorylationSH2 domain-dependent mannerPleckstrin homology domain-containing adaptor proteinDomain-containing adaptor proteinDomain-dependent mannerReceptor substrate-1Skeletal muscleSH2 domainHomology 2Adaptor proteinReceptor activationSubstrate-1Physiological roleCultured cellsGlucose homeostasisERK1/2 pathwayDependent insulin resistancePhysiological enhancerSystemic deletionPhosphorylationIRS2Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity
Fujii N, Boppart M, Dufresne S, Crowley P, Jozsi A, Sakamoto K, Yu H, Aschenbach W, Kim S, Miyazaki H, Rui L, White M, Hirshman M, Goodyear L. Overexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity. American Journal Of Physiology - Cell Physiology 2004, 287: c200-c208. PMID: 15013949, DOI: 10.1152/ajpcell.00415.2003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDown-RegulationElectroporationEnzyme ActivationGene Transfer TechniquesGlycogen SynthaseHumansInjections, IntramuscularInsulin Receptor Substrate ProteinsMiceMice, KnockoutMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9Mitogen-Activated Protein KinasesMuscle ContractionMuscle ProteinsMuscle, SkeletalPhosphoproteinsPhosphorylationSerineTyrosineConceptsGlycogen synthase activityMouse skeletal muscleS6 kinasePhosphorylation stateJNK signalingSynthase activityJNK activityProtein kinase B/AktJNK overexpressionGlycogen synthase kinase-3Skeletal muscleExtracellular signal-regulated kinase 1/2Signal-regulated kinase 1/2P70 S6 kinaseInsulin-stimulated glycogen synthase activitySynthase kinase-3P90 S6 kinaseBasal phosphorylation stateGlycogen synthase activationSitu muscle contractionBiological functionsTerminal kinaseKinase 3JNK activationKinase 1/2
2003
Nutrient-dependent and Insulin-stimulated Phosphorylation of Insulin Receptor Substrate-1 on Serine 302 Correlates with Increased Insulin Signaling*
Giraud J, Leshan R, Lee Y, White M. Nutrient-dependent and Insulin-stimulated Phosphorylation of Insulin Receptor Substrate-1 on Serine 302 Correlates with Increased Insulin Signaling*. Journal Of Biological Chemistry 2003, 279: 3447-3454. PMID: 14623899, DOI: 10.1074/jbc.m308631200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAndrostadienesAnimalsBlotting, WesternBromodeoxyuridineCell DivisionCell LineCHO CellsCricetinaeCulture Media, Serum-FreeDose-Response Relationship, DrugEnzyme InhibitorsGlucoseGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaInsulinInsulin Receptor Substrate ProteinsJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein KinasesMolecular Sequence DataMutagenesis, Site-DirectedMutationPhosphoproteinsPhosphorylationPoint MutationPrecipitin TestsRatsSerineSignal TransductionSirolimusTime FactorsWortmanninConceptsInsulin/IGFIRS-1Insulin-stimulated signal transductionInsulin receptor substrate IRS-1Ser/Thr phosphorylationSequence-specific polyclonal antibodiesInsulin-stimulated tyrosine phosphorylationInsulin receptor substrate-1Synthase kinase-3beta phosphorylationSubstrate IRS-1IRS-1-mediated signalingRibosomal S6 proteinC-Jun kinaseInsulin-stimulated phosphorylationReceptor substrate-1IGF-I stimulationThr phosphorylationKinase associatesP85 bindingPhosphorylated residuesSignal transductionInsulin-stimulated AktTyrosine phosphorylationS6 proteinNutrient availability
2002
c-Jun N-terminal Kinase (JNK) Mediates Feedback Inhibition of the Insulin Signaling Cascade*
Lee Y, Giraud J, Davis R, White M. c-Jun N-terminal Kinase (JNK) Mediates Feedback Inhibition of the Insulin Signaling Cascade*. Journal Of Biological Chemistry 2002, 278: 2896-2902. PMID: 12417588, DOI: 10.1074/jbc.m208359200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineConsensus SequenceCulture Media, ConditionedHumansInsulinInsulin Receptor Substrate ProteinsJNK Mitogen-Activated Protein KinasesMiceMice, KnockoutMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9Mitogen-Activated Protein KinasesMolecular Sequence DataPhosphoproteinsPhosphorylationRatsSignal TransductionTransfectionConceptsC-Jun N-terminal kinaseN-terminal kinaseDirect bindingInsulin-stimulated tyrosine phosphorylationInsulin receptor substrate-1Interaction of JNKInsulin Signaling CascadeReceptor substrate-1Mouse embryo fibroblastsActivation of JNKFeedback inhibitionNegative feedback regulatorPhosphorylation of IRS1Cellular proteinsCell-permeable peptideTyrosine phosphorylationInsulin signalSignaling cascadesIRS1 proteinJNK activitySubstrate-1Insulin stimulationEmbryo fibroblastsPhosphorylationAkt phosphorylation
2001
Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action*
Aguirre V, Werner E, Giraud J, Lee Y, Shoelson S, White M. Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action*. Journal Of Biological Chemistry 2001, 277: 1531-1537. PMID: 11606564, DOI: 10.1074/jbc.m101521200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnisomycinAnti-Bacterial AgentsCell LineHumansInsulinInsulin Receptor Substrate ProteinsMitogen-Activated Protein Kinase 8Mitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationRatsReceptor, InsulinRecombinant Fusion ProteinsSignal TransductionTumor Necrosis Factor-alphaTwo-Hybrid System TechniquesConceptsInsulin receptor substrate-1Phosphotyrosine-binding (PTB) domainInsulin receptorPotential phosphorylation sitesPhosphorylation of Ser307Stress-activated kinasesInsulin-stimulated kinasesReceptor substrate-1Insulin signal transductionPTB domainMAPK cascadePhosphorylation sitesMyeloid progenitor cellsSignal transductionSerine residuesCatalytic domainSerine phosphorylationDomain functionsSubstrate-1Insulin stimulationCell backgroundPhosphorylationProgenitor cellsGeneral mechanismMechanism of inhibitionRegulation of Insulin/Insulin-like Growth Factor-1 Signaling by Proteasome-mediated Degradation of Insulin Receptor Substrate-2*
Rui L, Fisher T, Thomas J, White M. Regulation of Insulin/Insulin-like Growth Factor-1 Signaling by Proteasome-mediated Degradation of Insulin Receptor Substrate-2*. Journal Of Biological Chemistry 2001, 276: 40362-40367. PMID: 11546773, DOI: 10.1074/jbc.m105332200.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAnimalsCarcinoma, HepatocellularDiabetes Mellitus, Type 2Down-RegulationFeedbackFibroblastsHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsLiver Neoplasms, ExperimentalMiceMitogen-Activated Protein KinasesOsmotic PressurePeptide HydrolasesPhosphatidylinositol 3-KinasesPhosphoproteinsProteasome Endopeptidase ComplexProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptor, InsulinSignal TransductionTOR Serine-Threonine KinasesTumor Cells, CulturedUbiquitinConceptsInsulin-like growth factor-1Insulin/IGFMouse embryo fibroblastsProteasome-mediated degradationIRS-2Embryo fibroblastsInsulin/insulin-like growth factor-1 signalingInsulin receptor substrate (IRS) proteinsUbiquitin/proteasome-mediated degradationNovel negative feedback mechanismInsulin-like growth factor-1 signalingInsulin receptor substrate 2Inhibitor of phosphatidylinositolIRS-1 activationPeripheral insulin actionIGF-1 treatmentReceptor tyrosine kinasesHomologous receptor tyrosine kinasesGrowth factor-1IRS proteinsSubstrate proteinsBeta-cell survivalOsmotic stressTyrosine kinaseIRS-1Regulation of Protein Synthesis by Insulin Through IRS-1
Mendez R, Welsh G, Kleijn M, Myers M, White M, Proud C, Rhoads R. Regulation of Protein Synthesis by Insulin Through IRS-1. Progress In Molecular And Subcellular Biology 2001, 26: 49-93. PMID: 11575167, DOI: 10.1007/978-3-642-56688-2_3.Peer-Reviewed Original ResearchAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell LineEnzyme ActivationEukaryotic Initiation Factor-2BGlycogen Synthase Kinase 3HumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMiceMitogen-Activated Protein KinasesModels, BiologicalPhosphatidylinositol 3-KinasesPhosphoproteinsProtein BiosynthesisProtein KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesRatsReceptor, InsulinSignal TransductionSirolimusTOR Serine-Threonine Kinases
2000
The c-Jun NH2-terminal Kinase Promotes Insulin Resistance during Association with Insulin Receptor Substrate-1 and Phosphorylation of Ser307 *
Davis R, Aguirre V, Uchida T, Yenush L, White M. The c-Jun NH2-terminal Kinase Promotes Insulin Resistance during Association with Insulin Receptor Substrate-1 and Phosphorylation of Ser307 *. Journal Of Biological Chemistry 2000, 275: 9047-9054. PMID: 10722755, DOI: 10.1074/jbc.275.12.9047.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnisomycinCHO CellsCricetinaeHumansInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein KinasesMolecular Sequence DataPhosphoproteinsPhosphorylationProtein BindingReceptor, InsulinRecombinant ProteinsSerineSignal TransductionTumor Necrosis Factor-alphaConceptsInsulin-stimulated tyrosine phosphorylationIRS-1Serine 307Tyrosine phosphorylationInsulin receptor substrate-1IRS-1 functionSignal transduction cascadePhosphorylation of Ser307Receptor substrate-1Chinese hamster ovary cellsIRS proteinsActivity of JNKJNK associatesPhosphorylation sitesHamster ovary cellsTransduction cascadeSerine phosphorylationTerminal kinaseSubstrate-1PhosphorylationStrong activatorPromotes Insulin ResistanceJNK phosphorylationOvary cellsJNK
1999
Stimulation of pancreatic beta-cell proliferation by growth hormone is glucose-dependent: signal transduction via janus kinase 2 (JAK2)/signal transducer and activator of transcription 5 (STAT5) with no crosstalk to insulin receptor substrate-mediated mitogenic signalling.
Cousin S, Hügl S, Myers M, White M, Reifel-Miller A, Rhodes C. Stimulation of pancreatic beta-cell proliferation by growth hormone is glucose-dependent: signal transduction via janus kinase 2 (JAK2)/signal transducer and activator of transcription 5 (STAT5) with no crosstalk to insulin receptor substrate-mediated mitogenic signalling. Biochemical Journal 1999, 344 Pt 3: 649-58. PMID: 10585851, PMCID: PMC1220686, DOI: 10.1042/0264-6021:3440649.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCell DivisionCell LineDNA-Binding ProteinsGlucoseGRB2 Adaptor ProteinGrowth HormoneInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsIslets of LangerhansJanus Kinase 2Milk ProteinsMitogen-Activated Protein KinasesPhosphoproteinsPhosphorylationProteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsRibosomal Protein S6 KinasesShc Signaling Adaptor ProteinsSignal TransductionSon of Sevenless Protein, DrosophilaSrc Homology 2 Domain-Containing, Transforming Protein 1STAT5 Transcription FactorTrans-ActivatorsConceptsINS-1 cell proliferationSignal transduction pathwaysSignal transductionCell proliferationKinase 2Sevenless-1 proteinMitogenic signal transduction pathwaysJAK2/STAT5 pathwayMitogen-activated protein kinaseInsulin receptor substrateBeta-cell proliferationRat growth hormoneJAK2/STAT5Pancreatic beta cell proliferationMitogenic signalingS6 kinaseProtein kinaseProtein associationTranscription 5Beta-cell lineReceptor substrateDifferent mitogenicRat beta-cell lineDownstream activationIRS-2