2018
Receptor Tyrosine Kinases and the Insulin Signaling System
White M. Receptor Tyrosine Kinases and the Insulin Signaling System. Endocrinology 2018, 121-155. DOI: 10.1007/978-3-319-44675-2_7.Peer-Reviewed Original ResearchProtein tyrosine kinasesTyrosine kinaseExtracellular ligand-binding domainLarge multigene familyRTK family membersInsulin Signaling SystemCell-cell interactionsLigand-binding domainReceptor tyrosine kinasesSystemic nutrient homeostasisPolypeptide growth factorsAspects of metabolismMultigene familyHuman genomeNutrient homeostasisPlasma membraneIntracellular signalsMetabolic regulationSignaling systemInsulin receptorBroader roleHeterologous regulationCell proliferationKinaseGrowth factor
2017
Receptor Tyrosine Kinases and the Insulin Signaling System
White M. Receptor Tyrosine Kinases and the Insulin Signaling System. Endocrinology 2017, 1-34. DOI: 10.1007/978-3-319-27318-1_7-1.Peer-Reviewed Original ResearchProtein tyrosine kinasesTyrosine kinaseExtracellular ligand-binding domainLarge multigene familyRTK family membersInsulin Signaling SystemCell-cell interactionsLigand-binding domainReceptor tyrosine kinasesSystemic nutrient homeostasisPolypeptide growth factorsAspects of metabolismMultigene familyHuman genomeNutrient homeostasisPlasma membraneIntracellular signalsMetabolic regulationSignaling systemInsulin receptorBroader roleHeterologous regulationCell proliferationKinaseGrowth factor
2013
Genetic Inactivation of Pyruvate Dehydrogenase Kinases Improves Hepatic Insulin Resistance Induced Diabetes
Tao R, Xiong X, Harris R, White M, Dong X. Genetic Inactivation of Pyruvate Dehydrogenase Kinases Improves Hepatic Insulin Resistance Induced Diabetes. PLOS ONE 2013, 8: e71997. PMID: 23940800, PMCID: PMC3733847, DOI: 10.1371/journal.pone.0071997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDiabetes Mellitus, ExperimentalGene Expression Regulation, EnzymologicGene SilencingGlucose IntoleranceGlucose Tolerance TestInsulin Receptor Substrate ProteinsInsulin ResistanceLiverMiceMice, KnockoutOrgan SpecificityProtein Serine-Threonine KinasesPyruvate Dehydrogenase Acetyl-Transferring KinaseConceptsPyruvate dehydrogenase kinasePDK4 geneGene knockdownDehydrogenase kinasePDK4 gene expressionMitochondrial pyruvate dehydrogenasePdk geneGene attributesPDK2 genesGene inactivationGene expressionGenetic inactivationPyruvate dehydrogenaseGenesInsulin receptorMetabolic analysisSpecific shRNAGene deletionGenetic backgroundHepatic insulin receptorNull miceKinasePDK2KnockdownCritical role
2012
Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2
Copps K, White M. Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2. Diabetologia 2012, 55: 2565-2582. PMID: 22869320, PMCID: PMC4011499, DOI: 10.1007/s00125-012-2644-8.Peer-Reviewed Original ResearchConceptsInsulin receptor substrateT phosphorylationReceptor substrateSerine/threonine residuesSerine/threonine phosphorylationInsulin receptor tyrosine kinaseInsulin-stimulated kinasesReceptor tyrosine kinasesThreonine phosphorylationThreonine residuesNegative regulationTyrosine kinasePhosphorylationCultured cellsKinaseMetabolic diseasesIRS2IRS1Hormonal controlKey targetAltered patternTail regionComplex mechanismsRegulationDysregulation
2011
Mechanisms of Insulin Action
White M, White M. Mechanisms of Insulin Action. 2011, 19-38. DOI: 10.1007/978-1-4614-1028-7_2.Peer-Reviewed Original ResearchInsulin-like growth factor 2Receptor tyrosine kinasesTyrosine kinaseInsulin-like signalingInsulin-like peptidesG protein-coupled receptorsInsulin-like growth factor-1Caenorhabditis elegansEnvironmental signalsHuman genomeFruit flyRelease of nutrientsGrowth factor 2Factor 1Factor 2Somatic growthKinaseLower animalsGrowth factor-1Common mechanismSimilar peptidesInsulin actionWide arrayMetabolismMetazoansInsulin 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
1998
The IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Molecular And Cellular Biochemistry 1998, 182: 3-11. PMID: 9609109, DOI: 10.1023/a:1006806722619.Peer-Reviewed Original ResearchConceptsIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetesThe IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Developments In Molecular And Cellular Biochemistry 1998, 3-11. DOI: 10.1007/978-1-4615-5647-3_1.Peer-Reviewed Original ResearchIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetesThe IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action
White M, Yenush L. The IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action. Current Topics In Microbiology And Immunology 1998, 228: 179-208. PMID: 9401207, DOI: 10.1007/978-3-642-80481-6_8.Peer-Reviewed Original ResearchConceptsTyrosine phosphorylationSrc homology 2 domainTyrosine autophosphorylation sitesProtein-lipid interactionsAssembly of multicomponentSH2 proteinAutophosphorylation sitesPH domainSpecific membrane receptorsCytosolic substratesReceptor kinaseTyrosine autophosphorylationTransmembrane signalsCellular substratesCytokine receptorsActivity of receptorsMembrane receptorsEarly stepsPhosphorylationProteinKinaseGrowth factorCytokine actionReceptorsCascade
1997
Heterologous Pleckstrin Homology Domains Do Not Couple IRS-1 to the Insulin Receptor*
Burks D, Pons S, Towery H, Smith-Hall J, Myers M, Yenush L, White M. Heterologous Pleckstrin Homology Domains Do Not Couple IRS-1 to the Insulin Receptor*. Journal Of Biological Chemistry 1997, 272: 27716-27721. PMID: 9346913, DOI: 10.1074/jbc.272.44.27716.Peer-Reviewed Original ResearchConceptsIRS-1 proteinPleckstrin homology domainPH domainIRS proteinsInsulin receptorIRS-1Homology domainTyrosine phosphorylationInsulin receptor tyrosine kinaseBeta-adrenergic receptor kinaseReceptor tyrosine kinasesNPEY motifPhospholipase CgammaReceptor kinaseTyrosine kinaseCommon functionProteinKinasePhosphorylationReceptorsDomainCgammaSpectrinMotifHigh levels
1996
Growth Hormone, Interferon-γ, and Leukemia Inhibitory Factor Utilize Insulin Receptor Substrate-2 in Intracellular Signaling*
Argetsinger L, Norstedt G, Billestrup N, White M, Carter-Su C. Growth Hormone, Interferon-γ, and Leukemia Inhibitory Factor Utilize Insulin Receptor Substrate-2 in Intracellular Signaling*. Journal Of Biological Chemistry 1996, 271: 29415-29421. PMID: 8910607, DOI: 10.1074/jbc.271.46.29415.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCHO CellsCricetinaeGrowth InhibitorsHuman Growth HormoneHumansInsulin Receptor Substrate ProteinsInterferon-gammaInterleukin-6Intracellular Signaling Peptides and ProteinsLeukemia Inhibitory FactorLymphokinesMicePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Signal TransductionTyrosineConceptsInsulin receptor substrate 2Tyrosyl phosphorylationLeukemia inhibitory factorProtein tyrosine phosphatase SHP2Substrate 2JAK2 associationPhosphatase SHP2Regulatory subunitJAK kinasesMaximal phosphorylationTyrosine phosphorylationTyrosine residuesIntracellular signalingPhosphorylationMultiple membersGH receptorInhibitory factorCytokine familyGrowth hormoneReceptorsSHP2KinasePhosphatidylinositolSubstantial signalThe 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 associationComplexesKinaseReceptorsP85
1991
The Juxtamembrane Regions of the Epidermal Growth Factor Receptor and gpl85 erbB-2 Determine the Specificity of Signal Transduction
Segatto O, Lonardo F, Wexler D, Fazioli F, Pierce J, Bottaro D, White M, Di Fiore P. The Juxtamembrane Regions of the Epidermal Growth Factor Receptor and gpl85 erbB-2 Determine the Specificity of Signal Transduction. Molecular And Cellular Biology 1991, 11: 3191-3202. DOI: 10.1128/mcb.11.6.3191-3202.1991.Peer-Reviewed Original ResearchEpidermal growth factor receptorSignal transductionSpecificity of substrate recognitionErbB-2Specificity of signal transductionAmino-terminal halfDeletion of residuesMitogenic signaling pathwaysMitogenic signal transductionEGFR kinaseGrowth factor receptorSubstrate recognitionTyrosine kinase domainJuxtamembrane regionKinase domainStructural homologyKinase propertiesFactor receptorMutation analysisSignaling pathwayTyrosine kinaseChimeric moleculesKinaseTyrosineTransduction