2013
Serine Phosphorylation Sites on IRS2 Activated by Angiotensin II and Protein Kinase C To Induce Selective Insulin Resistance in Endothelial Cells
Park K, Li Q, Rask-Madsen C, Mima A, Mizutani K, Winnay J, Maeda Y, D'Aquino K, White M, Feener E, King G. Serine Phosphorylation Sites on IRS2 Activated by Angiotensin II and Protein Kinase C To Induce Selective Insulin Resistance in Endothelial Cells. Molecular And Cellular Biology 2013, 33: 3227-3241. PMID: 23775122, PMCID: PMC3753901, DOI: 10.1128/mcb.00506-13.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsCattleCell LineEndothelial CellsEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceMaleMiceMice, TransgenicPhosphatidylinositol 3-KinasesPhosphorylationProtein Kinase CProtein Kinase C betaRatsRats, ZuckerSerineTetradecanoylphorbol AcetateThreonineTyrosineNerve Growth Factor Receptor TrkA, a New Receptor in Insulin Signaling Pathway in PC12 Cells*
Geetha T, Rege S, Mathews S, Meakin S, White M, Babu J. Nerve Growth Factor Receptor TrkA, a New Receptor in Insulin Signaling Pathway in PC12 Cells*. Journal Of Biological Chemistry 2013, 288: 23807-23813. PMID: 23749991, PMCID: PMC3745327, DOI: 10.1074/jbc.m112.436279.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsEnzyme ActivationGlucoseHumansInsulinInsulin Receptor Substrate ProteinsMitogen-Activated Protein Kinase 7Molecular Sequence DataNerve Growth FactorPC12 CellsPhosphorylationPhosphotyrosineProtein BindingProto-Oncogene Proteins c-aktRatsReceptor, InsulinReceptor, trkASignal TransductionConceptsInsulin receptor substrate-1Insulin receptorPC12 cellsTrkA kinase domainTransmembrane receptor tyrosine kinaseKinase-inactive mutantInsulin Signaling PathwayReceptor substrate-1Nerve growth factor receptor TrkAReceptor tyrosine kinasesNerve growth factorActivation of AktNPXY motifKinase domainTyrosine phosphorylationSubstrate-1Regulatory loopTyrosine kinaseSignaling pathwaysGrowth factorNew receptorsReceptor TrkACellsPathwayTrkA
2011
Inhibition of Insulin Signaling in Endothelial Cells by Protein Kinase C-induced Phosphorylation of p85 Subunit of Phosphatidylinositol 3-Kinase (PI3K)*
Maeno Y, Li Q, Park K, Rask-Madsen C, Gao B, Matsumoto M, Liu Y, Wu I, White M, Feener E, King G. Inhibition of Insulin Signaling in Endothelial Cells by Protein Kinase C-induced Phosphorylation of p85 Subunit of Phosphatidylinositol 3-Kinase (PI3K)*. Journal Of Biological Chemistry 2011, 287: 4518-4530. PMID: 22158866, PMCID: PMC3281670, DOI: 10.1074/jbc.m111.286591.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCells, CulturedClass Ia Phosphatidylinositol 3-KinaseEndothelial CellsEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMetabolic DiseasesNitric Oxide Synthase Type IIIPhosphorylationProtein Kinase CProto-Oncogene Proteins c-aktSignal TransductionVascular Endothelial Growth Factor AConceptsP85/PI3KPI3KPKC activationInsulin receptor substrateProtein kinase C activationEndothelial nitric oxide synthaseProtein kinase CAkt/endothelial nitric oxide synthaseKinase C activationPI3K/Akt pathwayP85 subunitDeletion mutantsGeneral activatorTyrosine phosphorylationReceptor substrateEndothelial cellsInsulin signalingInsulin activationKinase CAkt pathwayPhosphorylationC activationThr-86SignalingIRS1Insulin Receptor Substrates Irs1 and Irs2 Coordinate Skeletal Muscle Growth and Metabolism via the Akt and AMPK Pathways
Long Y, Cheng Z, Copps K, White M. Insulin Receptor Substrates Irs1 and Irs2 Coordinate Skeletal Muscle Growth and Metabolism via the Akt and AMPK Pathways. Molecular And Cellular Biology 2011, 31: 430-441. PMID: 21135130, PMCID: PMC3028618, DOI: 10.1128/mcb.00983-10.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsBody CompositionBody WeightEnzyme ActivationForkhead Transcription FactorsGlucoseHomeostasisIn Vitro TechniquesInsulinInsulin Receptor Substrate ProteinsLactic AcidMiceMice, KnockoutModels, BiologicalMuscle, SkeletalMyocardiumOrgan SizeOrgan SpecificityProto-Oncogene Proteins c-aktSignal TransductionUp-RegulationConceptsSkeletal muscle growthMdKO miceMuscle growthElevated AMP/ATP ratioInsulin-receptor substrate IRS1AMP/ATP ratioSkeletal muscleInsulin receptor substrateMuscle creatine kinaseSubstrates IRS1Insulin-stimulated glucose uptakeProtein kinaseNutrient availabilityReceptor substrateCarboxylase phosphorylationFatty acid oxidationAMPK pathwayMetabolic homeostasisATP ratioIRS1Impaired growthKinaseAmino acid releaseSkeletal muscle massAtrogene expression
2005
Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: Role of IRS phosphorylation
Zhang Q, Carter E, Ma B, White M, Fischman A, Tompkins R. Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: Role of IRS phosphorylation. Life Sciences 2005, 77: 3068-3077. PMID: 15982669, DOI: 10.1016/j.lfs.2005.02.034.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBurnsDisease Models, AnimalEnzyme ActivationHindlimbInsulin Receptor Substrate ProteinsInsulin ResistanceJNK Mitogen-Activated Protein KinasesMaleMAP Kinase Kinase 4MiceMitogen-Activated Protein Kinase KinasesMuscle, SkeletalPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptor, InsulinSignal TransductionConceptsInsulin receptor substrate-1Burn-induced insulin resistanceAkt kinase activityIRS-1 proteinSAPK/JNKSerine 307Kinase activitySkeletal muscleReceptor substrate-1Murine skeletal muscleHind limb skeletal muscleStress kinasesKey proteinsSubstrate-1Biochemical basisPhosphorylationIRS phosphorylationKinase enzymeProteinEnzyme activityJNKLimb skeletal muscleProtein contentInsulin resistanceKinase
2004
Signaling Pathways: The Benefits of Good Communication
Fisher T, White M. Signaling Pathways: The Benefits of Good Communication. Current Biology 2004, 14: r1005-r1007. PMID: 15589136, DOI: 10.1016/j.cub.2004.11.024.Peer-Reviewed Original ResearchOverexpression 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
2001
Regulation 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
1999
Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade.
Griffin ME, Marcucci MJ, Cline GW, Bell K, Barucci N, Lee D, Goodyear LJ, Kraegen EW, White MF, Shulman GI. Free fatty acid-induced insulin resistance is associated with activation of protein kinase C theta and alterations in the insulin signaling cascade. Diabetes 1999, 48: 1270-1274. PMID: 10342815, DOI: 10.2337/diabetes.48.6.1270.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDeoxyglucoseEnzyme ActivationFatty Acids, NonesterifiedInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIsoenzymesMagnetic Resonance SpectroscopyMaleMuscle, SkeletalPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Kinase CProtein Kinase C-thetaRatsRats, Sprague-DawleySignal TransductionTyrosineZinc FingersConceptsProtein kinase C thetaGlucose transport activityInsulin resistanceMuscle glycogen synthesisFree fatty acidsC thetaInsulin-stimulated insulin receptor substrateInsulin-stimulated IRS-1 tyrosine phosphorylationTransport activityIRS-1 tyrosine phosphorylationReduced glucose transport activityInsulin-stimulated muscle glucose metabolismFatty acid-induced insulin resistance
1998
The COOH-terminal Tyrosine Phosphorylation Sites on IRS-1 Bind SHP-2 and Negatively Regulate Insulin Signaling*
Myers M, Mendez R, Shi P, Pierce J, Rhoads R, White M. The COOH-terminal Tyrosine Phosphorylation Sites on IRS-1 Bind SHP-2 and Negatively Regulate Insulin Signaling*. Journal Of Biological Chemistry 1998, 273: 26908-26914. PMID: 9756938, DOI: 10.1074/jbc.273.41.26908.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCHO CellsCricetinaeEnzyme ActivationHumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein BindingProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesRatsSignal TransductionTyrosineConceptsSHP-2Tyrosine phosphorylationIRS-1Terminal tyrosine phosphorylation sitesTyrosine-phosphorylated motifsTyrosine phosphorylation sitesImportant regulatory eventInsulin receptor substrateProtein kinase activationSH2 domainGrb-2Phosphorylation sitesDownstream signal transmissionNumerous growth factorsRegulatory eventsReceptor substrateKinase activationInsulin signalingTyrosine kinaseInsulin stimulationCytokine receptorsProtein synthesisPhosphorylationTerminal tyrosineDownstream signalsInsulin-like Growth Factor I (IGF-I)-stimulated Pancreatic β-Cell Growth Is Glucose-dependent SYNERGISTIC ACTIVATION OF INSULIN RECEPTOR SUBSTRATE-MEDIATED SIGNAL TRANSDUCTION PATHWAYS BY GLUCOSE AND IGF-I IN INS-1 CELLS*
Hügl S, White M, Rhodes C. Insulin-like Growth Factor I (IGF-I)-stimulated Pancreatic β-Cell Growth Is Glucose-dependent SYNERGISTIC ACTIVATION OF INSULIN RECEPTOR SUBSTRATE-MEDIATED SIGNAL TRANSDUCTION PATHWAYS BY GLUCOSE AND IGF-I IN INS-1 CELLS*. Journal Of Biological Chemistry 1998, 273: 17771-17779. PMID: 9651378, DOI: 10.1074/jbc.273.28.17771.Peer-Reviewed Original ResearchConceptsInsulin-like growth factor IGrowth factor IBeta-cell proliferationINS-1 cell proliferationCell proliferationFactor IMM glucoseCombination of IGFPancreatic β-cell growthPancreatic beta-cell lineBeta-cell lineΒ-cell growthINS-1 cellsNM IGFBeta-cell mitogenesisCertain growth factorsSignaling mechanismSignal transduction pathwaysGlucose metabolismIGFCell proliferation rateGrowth factorIRS-2Transduction pathwaysGlucose concentrationInsulin receptor substrate (IRS) proteins IRS-1 and IRS-2 differential signaling in the insulin/insulin-like growth factor-I pathways in fetal brown adipocytes.
Valverde A, Lorenzo M, Pons S, White M, Benito M. Insulin receptor substrate (IRS) proteins IRS-1 and IRS-2 differential signaling in the insulin/insulin-like growth factor-I pathways in fetal brown adipocytes. Endocrinology 1998, 12: 688-97. PMID: 9605931, DOI: 10.1210/mend.12.5.0106.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdipocytesAdipose Tissue, BrownAmino Acid SequenceAnimalsEnzyme ActivationFetusGRB2 Adaptor ProteinInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein BindingProteinsRatsRats, WistarReceptor, InsulinSignal TransductionSrc Homology DomainsTyrosineConceptsInsulin/IGFInsulin receptor substrateIRS-1IRS-2Shc proteinsTyrosine phosphorylationInsulin receptor substrate (IRS) proteinsInsulin/insulin-like growth factorFetal rat brown adipocytesIRS-2-associated phosphatidylinositolIRS-2 tyrosine phosphorylationFetal brown adipocytesProtein kinase signal pathwayBrown adipocytesKinase signal pathwayBrown adipocyte proliferationInsulin/insulinSubstrate proteinsSH2 domainGrb-2Thermogenic differentiationFetal brown adipose tissueReceptor substrateFusion proteinInsulin-like growth factor
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 linkPhosphorylationTraffickingSubunitsCa2Requirement of Protein Kinase Cζ for Stimulation of Protein Synthesis by Insulin
Mendez R, Kollmorgen G, White M, Rhoads R. Requirement of Protein Kinase Cζ for Stimulation of Protein Synthesis by Insulin. Molecular And Cellular Biology 1997, 17: 5184-5192. PMID: 9271396, PMCID: PMC232369, DOI: 10.1128/mcb.17.9.5184.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCalcium-Calmodulin-Dependent Protein KinasesEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMiceOligonucleotides, AntisensePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)Protein BiosynthesisProtein Kinase CProtein Serine-Threonine KinasesProto-Oncogene Proteins c-mycRibosomal Protein S6 KinasesConceptsGeneral protein synthesisPKC-zetaCell cycle progressionProtein synthesisIRS-1Insulin receptorCycle progressionGuanine nucleotide exchange factorsNucleotide exchange factorsInsulin-stimulated protein synthesisProto-oncogene AktTarget of rapamycinMitogen-activated protein kinaseInsulin-stimulated activationPKC zeta activationProtein kinase CζGrowth-regulating proteinsActive PKC-zetaPrevention of apoptosisExchange factorPhosphorylated substratesS6 kinaseProtein kinaseGab-1Ectopic expressionActivation of the phosphatidylinositol 3-kinase serine kinase by IFN-alpha.
Uddin S, Fish E, Sher D, Gardziola C, White M, Platanias L. Activation of the phosphatidylinositol 3-kinase serine kinase by IFN-alpha. The Journal Of Immunology 1997, 158: 2390-7. PMID: 9036989, DOI: 10.4049/jimmunol.158.5.2390.Peer-Reviewed Original ResearchConceptsSerine kinaseTreatment of cellsIRS-1Kinase assaysSerine kinase activityDual-specificity enzymeP85 regulatory subunitReceptor-generated signalsIRS-1 proteinJak-1 kinasesIFN-alpha-induced activationProtein associatesP85 subunitPhosphoaminoacid analysisRegulatory subunitSerine residuesSerine phosphorylationTyrosine phosphorylationTyk-2STAT-2MAP kinaseKinase activityPretreatment of cellsInhibitor wortmanninPhosphatidylinositol
1996
Insulin-induced egr-1 and c-fos Expression in 32D Cells Requires Insulin Receptor, Shc, and Mitogen-activated Protein Kinase, but Not Insulin Receptor Substrate-1 and Phosphatidylinositol 3-Kinase Activation*
Harada S, Smith R, Smith J, White M, Jarett L. Insulin-induced egr-1 and c-fos Expression in 32D Cells Requires Insulin Receptor, Shc, and Mitogen-activated Protein Kinase, but Not Insulin Receptor Substrate-1 and Phosphatidylinositol 3-Kinase Activation*. Journal Of Biological Chemistry 1996, 271: 30222-30226. PMID: 8939974, DOI: 10.1074/jbc.271.47.30222.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell LineCHO CellsCricetinaeDNA-Binding ProteinsEarly Growth Response Protein 1Enzyme ActivationEnzyme InhibitorsGene Expression RegulationGRB2 Adaptor ProteinImmediate-Early ProteinsInsulinInsulin Receptor Substrate ProteinsMicePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein KinasesProteinsProto-Oncogene Proteins c-fosReceptor, InsulinRNA, MessengerTranscription FactorsTyrosineConceptsC-fos expressionInsulin receptor substrate-1Egr-1 expressionInsulin receptorReceptor substrate-1Mitogen-activated protein kinase activationEgr-1Protein kinase activationMultiple signal transduction pathwaysBlot analysisEffect of insulinSignal transduction pathwaysSubstrate-1Tyrosine phosphorylationImmediate early gene Egr-1Mitogen-activated protein kinase kinase inhibitorWestern blot analysisProtein kinase kinase inhibitorInsulin receptor tyrosine phosphorylationInsulin treatmentKinase activationIRS-1 phosphorylationTransduction pathwaysKinase kinase inhibitorGene Egr-1YMXM Motifs and Signaling by an Insulin Receptor Substrate 1 Molecule without Tyrosine Phosphorylation Sites
Myers M, Zhang Y, Aldaz G, Grammer T, Glasheen E, Yenush L, Wang L, Sun X, Blenis J, Pierce J, White M. YMXM Motifs and Signaling by an Insulin Receptor Substrate 1 Molecule without Tyrosine Phosphorylation Sites. Molecular And Cellular Biology 1996, 16: 4147-4155. PMID: 8754813, PMCID: PMC231411, DOI: 10.1128/mcb.16.8.4147.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell DivisionCell LineDNA ReplicationEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMolecular Sequence DataMutagenesis, Site-DirectedPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein Serine-Threonine KinasesReceptor, InsulinRecombinant ProteinsRibosomal Protein S6 KinasesSignal TransductionStructure-Activity RelationshipConceptsTyrosine phosphorylation sitesPotential tyrosine phosphorylation sitesYMXM motifsPhosphorylation sitesIRS-1SH2 proteinTyrosine phosphorylationSrc homology 2 domainIRS-1 moleculeWild-type IRS-1Insulin receptor substrate-1Mitogen-activated protein kinaseInsulin-stimulated mitogenesisReceptor substrate-1IRS proteinsProtein kinaseMitogenic signalsMitogenic responseSubstrate-1Mitogenic sensitivityInsulin signalingInsulin stimulationPhosphotidylinositolRedundant motifsProteinThe Fyn Tyrosine Kinase Binds Irs-1 and Forms a Distinct Signaling Complex during Insulin Stimulation (∗)
Sun X, Pons S, Asano T, Myers M, Glasheen E, White M. The Fyn Tyrosine Kinase Binds Irs-1 and Forms a Distinct Signaling Complex during Insulin Stimulation (∗). Journal Of Biological Chemistry 1996, 271: 10583-10587. PMID: 8631859, DOI: 10.1074/jbc.271.18.10583.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCHO CellsCricetinaeDNA PrimersEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMiceMolecular Sequence DataPhosphoproteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-fynSignal TransductionSrc Homology DomainsSubstrate SpecificityConceptsSrc homology 2Grb-2Insulin stimulationTyrosine phosphorylation sitesInsulin/IGFSH2 domainSH2 proteinSignaling ComplexHomology 2Related Src kinasesPhosphorylation sitesIR-1Src kinaseExpression libraryP59fyn kinaseTyrosine residuesP59fynInsulin receptorIR proteinProteinSpecific associationComplexesKinaseReceptorsP85Tumor Necrosis Factor (TNF)-α Inhibits Insulin Signaling through Stimulation of the p55 TNF Receptor and Activation of Sphingomyelinase*
Peraldi P, Hotamisligil G, Buurman W, White M, Spiegelman B. Tumor Necrosis Factor (TNF)-α Inhibits Insulin Signaling through Stimulation of the p55 TNF Receptor and Activation of Sphingomyelinase*. Journal Of Biological Chemistry 1996, 271: 13018-13022. PMID: 8662983, DOI: 10.1074/jbc.271.22.13018.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdipocytesAnimalsAntigens, CDCell LineCeramidesEnzyme ActivationHumansInsulinInsulin Receptor Substrate ProteinsMicePhosphoproteinsPhosphorylationReceptor, InsulinReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISignal TransductionSphingomyelin PhosphodiesteraseTumor Necrosis Factor-alphaTyrosineConceptsInsulin receptor substrate-1Myeloid 32D cellsInsulin receptorP55 TNF receptorP75 TNF receptorTyrosine phosphorylationInhibits InsulinIRS-2Insulin-dependent tyrosine phosphorylationTNF receptorIRS-1 tyrosine phosphorylationTNF-alphaIR tyrosine kinaseReceptor substrate-1Tyrosine kinase activityNecrosis factorActivation of sphingomyelinaseSerine phosphorylationBiological functionsKinase activitySubstrate-1Tyrosine kinaseExogenous sphingomyelinaseMurine TNF-alphaTumor necrosis factorThe Drosophila Insulin Receptor Activates Multiple Signaling Pathways but Requires Insulin Receptor Substrate Proteins for DNA Synthesis
Yenush L, Fernandez R, Myers M, Grammer T, Sun X, Blenis J, Pierce J, Schlessinger J, White M. The Drosophila Insulin Receptor Activates Multiple Signaling Pathways but Requires Insulin Receptor Substrate Proteins for DNA Synthesis. Molecular And Cellular Biology 1996, 16: 2509-2517. PMID: 8628319, PMCID: PMC231240, DOI: 10.1128/mcb.16.5.2509.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell LineDNADrosophila melanogasterEnzyme ActivationHumansInsulinInsulin Receptor Substrate ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein Serine-Threonine KinasesReceptor, InsulinRecombinant ProteinsRibosomal Protein S6 KinasesSequence Homology, Amino AcidSignal TransductionThymidineConceptsDrosophila insulin receptorHuman insulin receptorInsulin receptor substrate (IRS) proteinsIRS-1Insulin receptorSubstrate proteinsTyrosine phosphorylation sitesMitogen-activated protein kinaseInsulin-stimulated mitogenesisMultiple signaling pathwaysIRS proteinsMammalian counterpartsYXXM motifsPhosphorylation sitesMammalian cellsTyrosine autophosphorylationProtein kinaseTyrosine phosphorylationSignaling pathwaysPhosphatidylinositolTerminal extensionDNA synthesisProteinHDIRP70S6k