Featured Publications
Mechanism of Insulin Action
White M. Mechanism of Insulin Action. 2024, 111-127. DOI: 10.1002/9781119697473.ch9.Peer-Reviewed Original ResearchReceptor tyrosine kinasesTyrosine kinaseGrowth factor signalingSecrete sufficient insulinDysregulated insulin signalingPancreatic beta cellsMuscle insulin resistanceEnvironmental signalsSignal transductionInsulin signalingMuscle-specific deletionSystemic insulin actionSystemic insulin resistanceAdequate insulin responseFactor signalingInsulin-like growth factor signalingPlasma membraneInsulin resistanceInsulin receptorLigand bindingBeta cellsMetabolic stressChronic insulin resistanceGlucose transportTransphosphorylation
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
2016
Mechanism of Insulin Action
White M. Mechanism of Insulin Action. 2016, 114-132. DOI: 10.1002/9781118924853.ch8.Peer-Reviewed Original ResearchInsulin-like signalingGenome-wide association studiesInsulin-like peptidesClassical insulin target tissuesInsulin-like growth factor 2Receptor tyrosine kinasesSimilar receptor tyrosine kinasesEnvironmental signalsHuman genomeInsulin target tissuesGenetic lociPancreatic β-cellsInsulin signalTyrosine kinaseAssociation studiesRelease of nutrientsConflicting signalsGrowth factor 2IGF signalingAnimal growthFactor 1Factor 2Insulin-like growth factor-1Β-cellsGenes
2014
Insulin and Metabolic Stress Stimulate Multisite Serine/Threonine Phosphorylation of Insulin Receptor Substrate 1 and Inhibit Tyrosine Phosphorylation*
Hançer N, Qiu W, Cherella C, Li Y, Copps K, White M. Insulin and Metabolic Stress Stimulate Multisite Serine/Threonine Phosphorylation of Insulin Receptor Substrate 1 and Inhibit Tyrosine Phosphorylation*. Journal Of Biological Chemistry 2014, 289: 12467-12484. PMID: 24652289, PMCID: PMC4007441, DOI: 10.1074/jbc.m114.554162.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnisomycinAntigens, CDBlotting, WesternCHO CellsCricetinaeCricetulusEnzyme InhibitorsHumansHypoglycemic AgentsInsulinInsulin Receptor Substrate ProteinsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktRatsReceptor, InsulinRibosomal Protein S6 Kinases, 70-kDaSerineSignal TransductionThapsigarginThreonineTOR Serine-Threonine KinasesTunicamycinTyrosineConceptsTyrosine phosphorylationPhospho-specific monoclonal antibodiesSerine/threonine phosphorylationInsulin receptor tyrosine kinasePI3KInsulin receptor substrate-1Insulin-stimulated cellsHuman insulin receptorIRS1 tyrosine phosphorylationReceptor substrate-1Metabolic stressReceptor tyrosine kinasesThreonine phosphorylationThreonine residuesS6 kinasePI3K inhibitionSubstrate-1Mechanistic targetTyrosine kinaseInsulin stimulationMEK pathwayKey substrateInsulin receptorPresence of inhibitorsCHO cells
2013
Nerve 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
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 arrayMetabolismMetazoans
2004
Insulin receptor substrate proteins and diabetes
Lee Y, White M. Insulin receptor substrate proteins and diabetes. Archives Of Pharmacal Research 2004, 27: 361-370. PMID: 15180298, DOI: 10.1007/bf02980074.Peer-Reviewed Original ResearchConceptsInsulin receptor substrate (IRS) proteinsSubstrate proteinsPancreatic β-cell growthInsulin/IGFIntracellular signaling cascadesReceptor tyrosine kinasesΒ-cell growthCell surface receptorsIRS proteinsGrowth factor actionProtein signalingSerine phosphorylationSignaling cascadesInsulin resistanceTyrosine kinaseInsulin-like growth factor actionIrs2 branchCell growthSurface receptorsFactor actionPeripheral insulin responsePeripheral insulin resistanceIRS2ProteinImportant mechanism
2002
Defective insulin secretion in pancreatic β cells lacking type 1 IGF receptor
Xuan S, Kitamura T, Nakae J, Politi K, Kido Y, Fisher P, Morroni M, Cinti S, White M, Herrera P, Accili D, Efstratiadis A. Defective insulin secretion in pancreatic β cells lacking type 1 IGF receptor. Journal Of Clinical Investigation 2002, 110: 1011-1019. PMID: 12370279, PMCID: PMC151144, DOI: 10.1172/jci15276.Peer-Reviewed Original ResearchConceptsType 1 IGF receptorBeta-cell massDefective insulin secretionInsulin secretionIGF receptorInsulin releaseInadequate compensatory increaseGlucose-dependent insulin releaseBeta-cell proliferationAge-dependent impairmentPancreatic β-cellsGlucose toleranceDecrease of glucoseBeta cellsType 2Compensatory increaseCell massΒ-cellsReceptor tyrosine kinasesSecretionCell proliferationAntiapoptotic roleReceptorsTyrosine kinaseConditional mutagenesis
2001
Regulation 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-1
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