Featured Publications
Elevated circulating follistatin associates with an increased risk of type 2 diabetes
Wu C, Borné Y, Gao R, López Rodriguez M, Roell W, Wilson J, Regmi A, Luan C, Aly D, Peter A, Machann J, Staiger H, Fritsche A, Birkenfeld A, Tao R, Wagner R, Canouil M, Hong M, Schwenk J, Ahlqvist E, Kaikkonen M, Nilsson P, Shore A, Khan F, Natali A, Melander O, Orho-Melander M, Nilsson J, Häring H, Renström E, Wollheim C, Engström G, Weng J, Pearson E, Franks P, White M, Duffin K, Vaag A, Laakso M, Stefan N, Groop L, De Marinis Y. Elevated circulating follistatin associates with an increased risk of type 2 diabetes. Nature Communications 2021, 12: 6486. PMID: 34759311, PMCID: PMC8580990, DOI: 10.1038/s41467-021-26536-w.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdipose TissueDiabetes Mellitus, Type 2FollistatinGenome-Wide Association StudyHepatocytesHumansInsulin ResistanceMiddle AgedNon-alcoholic Fatty Liver DiseaseConceptsAdipose tissue insulin resistanceTissue insulin resistanceType 2 diabetesFollistatin levelsGlucokinase regulatory protein geneFollistatin secretionHazard ratioInsulin resistanceNon-alcoholic fatty liver diseaseAdjusted hazard ratioFatty liver diseaseRisk of T2DFree fatty acid releaseFatty acid releaseIncident T2DLiver diseaseGenome-wide association studiesHuman adipocytesT2DAcid releaseStandard deviation increaseDiabetesSecretionRiskRegulatory protein geneTAZ inhibits glucocorticoid receptor and coordinates hepatic glucose homeostasis in normal physiological states
Xu S, Liu Y, Hu R, Wang M, Stöhr O, Xiong Y, Chen L, Kang H, Zheng L, Cai S, He L, Wang C, Copps K, White M, Miao J. TAZ inhibits glucocorticoid receptor and coordinates hepatic glucose homeostasis in normal physiological states. ELife 2021, 10: e57462. PMID: 34622775, PMCID: PMC8555985, DOI: 10.7554/elife.57462.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBlood GlucoseGluconeogenesisHomeostasisIntracellular Signaling Peptides and ProteinsLiverMice, KnockoutReceptors, GlucocorticoidConceptsGluconeogenic gene promotersBinding of GRGene promoterGlucocorticoid receptorGlucose homeostasisLigand-binding domainGlucose productionOverexpression of TAZHepatic glucose homeostasisWW domainsBlood glucose concentrationPhysiological fastingGluconeogenic genesGR response elementResponse elementNovel roleTAZNormal physiological stateGR transactivationPhysiological statePromoterMouse liverPericentral hepatocytesPathological statesGlucose concentration
2014
APPL1 Potentiates Insulin Sensitivity by Facilitating the Binding of IRS1/2 to the Insulin Receptor
Ryu J, Galan A, Xin X, Dong F, Abdul-Ghani M, Zhou L, Wang C, Li C, Holmes B, Sloane L, Austad S, Guo S, Musi N, DeFronzo R, Deng C, White M, Liu F, Dong L. APPL1 Potentiates Insulin Sensitivity by Facilitating the Binding of IRS1/2 to the Insulin Receptor. Cell Reports 2014, 7: 1227-1238. PMID: 24813896, PMCID: PMC4380268, DOI: 10.1016/j.celrep.2014.04.006.Peer-Reviewed Original Research
2010
Deletion of Irs2 causes reduced kidney size in mice: role for inhibition of GSK3β?
Carew R, Sadagurski M, Goldschmeding R, Martin F, White M, Brazil D. Deletion of Irs2 causes reduced kidney size in mice: role for inhibition of GSK3β? BMC Developmental Biology 2010, 10: 73. PMID: 20604929, PMCID: PMC2910663, DOI: 10.1186/1471-213x-10-73.Peer-Reviewed Original ResearchConceptsIrs2-/- miceYes-associated proteinKidney sizeΒ-cateninΒ-catenin targetsBody weight ratioImportant novel mediatorType 2 diabetesPostnatal day 5Mouse developmentInhibition of GSK3βOrgan sizeYAP activityYAP phosphorylationPituitary developmentDevelopmental defectsYAP levelsGlomerular densityRenal growthNeuronal proliferationAnalysis of insulinGlomerular numberConcomitant accumulationDay 5Kidney structure
2008
Inactivation of Hepatic Foxo1 by Insulin Signaling Is Required for Adaptive Nutrient Homeostasis and Endocrine Growth Regulation
Dong X, Copps K, Guo S, Li Y, Kollipara R, DePinho R, White M. Inactivation of Hepatic Foxo1 by Insulin Signaling Is Required for Adaptive Nutrient Homeostasis and Endocrine Growth Regulation. Cell Metabolism 2008, 8: 65-76. PMID: 18590693, PMCID: PMC2929667, DOI: 10.1016/j.cmet.2008.06.006.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsEndocrine GlandsFoodForkhead Transcription FactorsGrowthHomeostasisInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIntracellular Signaling Peptides and ProteinsLiverMiceMice, KnockoutNerve Tissue ProteinsPhosphoproteinsSignal TransductionConceptsInsulin signalingForkhead transcription factor FOXO1Insulin-regulated glucose homeostasisExpression of genesTranscription factor FOXO1Endocrine growth regulationNutrient homeostasisMetabolic genesStress resistancePerturbed expressionActive FoxO1Growth regulationLiver-specific deletionHepatic FoxO1Hepatic insulin resistanceBody sizePI3KHepatic Irs1FOXO1TranscriptomeSomatic growthDKO miceGenesSignalingHomeostasis
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 deletionPhosphorylationIRS2
2002
Specificity of Interleukin-2 Receptor γ Chain Superfamily Cytokines Is Mediated by Insulin Receptor Substrate-dependent Pathway*
Xiao H, Yin T, Wang X, Uchida T, Chung J, White M, Yang Y. Specificity of Interleukin-2 Receptor γ Chain Superfamily Cytokines Is Mediated by Insulin Receptor Substrate-dependent Pathway*. Journal Of Biological Chemistry 2002, 277: 8091-8098. PMID: 11788580, DOI: 10.1074/jbc.m106650200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsCell DivisionCell LineCytokinesDose-Response Relationship, DrugEnzyme InhibitorsGRB2 Adaptor ProteinInsulin Receptor Substrate ProteinsInterleukin-4Interleukin-9MicePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPlasmidsProtein BindingProtein Structure, TertiaryProteinsReceptors, Interleukin-2Signal TransductionTransfectionTyrosineConceptsIRS proteinsCytokine specificityIL-4-mediated functionsPleckstrin homology domainJak tyrosine kinasesUnique biological functionsPI3K activityPhosphotyrosine bindingHomology domainPH domainSHP-2Different structural domainsPhosphatidylinositol 3IL-4 stimulationBinding domainsIL-2 receptor gamma chainBiological functionsPathways workProliferative effectTyrosine kinaseIRS-2IRS-1Structural domainsAkt activationIRS-4
2001
Association of Insulin Receptor Substrate 1 (IRS-1) Y895 with Grb-2 Mediates the Insulin Signaling Involved in IRS-1-Deficient Brown Adipocyte Mitogenesis
Valverde A, Mur C, Pons S, Alvarez A, White M, Kahn C, Benito M. Association of Insulin Receptor Substrate 1 (IRS-1) Y895 with Grb-2 Mediates the Insulin Signaling Involved in IRS-1-Deficient Brown Adipocyte Mitogenesis. Molecular And Cellular Biology 2001, 21: 2269-2280. PMID: 11259577, PMCID: PMC86861, DOI: 10.1128/mcb.21.7.2269-2280.2001.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdipocytesAdipose Tissue, BrownAnimalsCells, CulturedGene DeletionGRB2 Adaptor ProteinInsulinInsulin Receptor Substrate ProteinsMiceMitosisPhosphoproteinsProteinsSignal TransductionConceptsMitogen-activated protein kinaseGrb-2Tyrosine phosphorylationIRS-1Brown adipocytesMAPK activationBrown adipocyte cell lineDNA synthesisActivation of MAPKWild-type IRS-1IRS-2 tyrosine phosphorylationShc tyrosine phosphorylationProtein kinase kinaseInhibition of phosphatidylinositolWild-type cell linesIRS-1 deficiencyInsulin-induced IRS-1Cell linesInsulin receptor substrate-1 (IRS-1) knockout miceAdipocyte cell lineG2/M phaseKinase kinaseMutant cellsProtein kinaseCell cycleIRS proteins and beta-cell function.
Burks D, White M. IRS proteins and beta-cell function. Diabetes 2001, 50: s140. PMID: 11272176, DOI: 10.2337/diabetes.50.2007.s140.Peer-Reviewed Original ResearchConceptsInsulin receptor substrateIRS proteinsIRS protein familyBeta-cell functionBeta-cell massClassical insulin target tissuesDownstream effector pathwaysPeripheral insulin resistanceIRS-2 geneInsulin resistanceProtein familyInsulin target tissuesReceptor substrateIRS-1Effector pathwaysPancreatic beta-cell massInsulin secretory reserveGrowth-promoting actionProteinBeta-cell dysfunctionSomatic growthType 2 diabetesCritical roleDiabetic phenotypeRegulation
2000
Tyrosine Dephosphorylation and Deactivation of Insulin Receptor Substrate-1 by Protein-tyrosine Phosphatase 1B POSSIBLE FACILITATION BY THE FORMATION OF A TERNARY COMPLEX WITH THE GRB2 ADAPTOR PROTEIN*
Goldstein B, Bittner-Kowalczyk A, White M, Harbeck M. Tyrosine Dephosphorylation and Deactivation of Insulin Receptor Substrate-1 by Protein-tyrosine Phosphatase 1B POSSIBLE FACILITATION BY THE FORMATION OF A TERNARY COMPLEX WITH THE GRB2 ADAPTOR PROTEIN*. Journal Of Biological Chemistry 2000, 275: 4283-4289. PMID: 10660596, DOI: 10.1074/jbc.275.6.4283.Peer-Reviewed Original ResearchConceptsInsulin receptor substrate-1Receptor substrate-1Tyrosine dephosphorylationAdaptor proteinSubstrate-1Tyrosine-phosphorylated IRS-1Src homology 2 domainSteady-state tyrosine phosphorylationAdaptor protein Grb2Grb2 adaptor proteinStable protein complexesProtein tyrosine phosphataseNovel molecular interactionInsulin signal transductionMolecular interactionsProtein Grb2Protein complexesP85 subunitSHP-2Overlay blotsP-nitrophenyl phosphateSignal transductionTyrosine phosphorylationPhosphorylation stateInactive PTP1BIRS-4 Mediates Protein Kinase B Signaling during Insulin Stimulation without Promoting Antiapoptosis
Uchida T, Myers M, White M. IRS-4 Mediates Protein Kinase B Signaling during Insulin Stimulation without Promoting Antiapoptosis. Molecular And Cellular Biology 2000, 20: 126-138. PMID: 10594015, PMCID: PMC85068, DOI: 10.1128/mcb.20.1.126-138.2000.Peer-Reviewed Original ResearchConceptsPKB/AktProtein kinase BIRS-1IRS-2IRS-4Insulin stimulationGrb-2Bad phosphorylationInsulin-stimulated mitogen-activated protein kinase activityInsulin receptor substrate (IRS) proteinsProtein kinase B signalingMitogen-activated protein kinase activityProtein kinase activityHuman insulin receptorPhosphorylation of BadKinase B signalingSubstrate proteinsMyeloid progenitor cellsApoptosis of cellsKinase activityKinase BPhosphatidylinositolInsulin receptorInterleukin-3Phosphorylation
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-2Differential Modulation of the Tyrosine Phosphorylation State of the Insulin Receptor by IRS (Insulin Receptor Subunit) Proteins
Solow B, Harada S, Goldstein B, Smith J, White M, Jarett L. Differential Modulation of the Tyrosine Phosphorylation State of the Insulin Receptor by IRS (Insulin Receptor Subunit) Proteins. Endocrinology 1999, 13: 1784-1798. PMID: 10517679, DOI: 10.1210/mend.13.10.0361.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsInsulinInsulin Receptor Substrate ProteinsMicePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Tyrosine PhosphatasesProteinsReceptor, InsulinRecombinant ProteinsSequence DeletionShc Signaling Adaptor ProteinsSignal TransductionSrc Homology 2 Domain-Containing, Transforming Protein 1Stem CellsTyrosineVanadatesConceptsInsulin receptor phosphorylationTyrosine kinase activityInsulin receptor tyrosine phosphorylationReceptor tyrosine phosphorylationTyrosine phosphorylationKinase activityIRS-1IRS-2Receptor phosphorylationInsulin receptorTyrosine-phosphorylated IRS-1Insulin stimulationProtein tyrosine phosphatase activityTyrosine phosphorylation stateProtein tyrosine phosphataseReceptor tyrosine kinase activityReceptor kinase activityInsulin receptor kinase activityInsulin receptor subunitsIRS proteinsPervanadate treatmentPhosphorylation stateDownstream eventsInsulin actionTyrosine residues
1998
Differential Regulation of Insulin Receptor Substrate-2 and Mitogen-Activated Protein Kinase Tyrosine Phosphorylation by Phosphatidylinositol 3-Kinase Inhibitors in SH-SY5Y Human Neuroblastoma Cells*This work was supported by NIH Grants R29-NS-32843 and R01-NS-36778, grants from the American Diabetes Association and Juvenile Diabetes Foundation (to E.L.F.), and a grant from the Millie Schembechler Adrenal Research Fund of the University of Michigan Comprehensive Cancer Center (to E.L.F. and P.S.L.).
Kim B, Leventhal P, White M, Feldman E. Differential Regulation of Insulin Receptor Substrate-2 and Mitogen-Activated Protein Kinase Tyrosine Phosphorylation by Phosphatidylinositol 3-Kinase Inhibitors in SH-SY5Y Human Neuroblastoma Cells*This work was supported by NIH Grants R29-NS-32843 and R01-NS-36778, grants from the American Diabetes Association and Juvenile Diabetes Foundation (to E.L.F.), and a grant from the Millie Schembechler Adrenal Research Fund of the University of Michigan Comprehensive Cancer Center (to E.L.F. and P.S.L.). Endocrinology 1998, 139: 4881-4889. PMID: 9832424, DOI: 10.1210/endo.139.12.6348.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportCalcium-Calmodulin-Dependent Protein KinasesElectrophoresis, Polyacrylamide GelEnzyme InhibitorsGRB2 Adaptor ProteinHumansInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsIsoenzymesMitogen-Activated Protein Kinase 1NeuritesNeuroblastomaPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsPhosphorylationProteinsShc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1Tumor Cells, CulturedTyrosineConceptsInsulin receptor substrate 2IRS-2 tyrosine phosphorylationMitogen-activated protein kinase activationTyrosine phosphorylationProtein kinase activationKinase activationSerine/threonine phosphorylationSubstrate 2Association of Grb2Neurite outgrowthSH-SY5Y human neuroblastomaThreonine phosphorylationNegative regulationSH-SY5Y human neuroblastoma cellsIRS-1Grb2Nervous system growthDifferential regulationPhosphorylationHuman neuroblastoma cellsNeuronal cellsPhosphatidylinositolPI 3Concentration-dependent mannerInsulin-like growth factor IThe 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 ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsDNA-Binding ProteinsHumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsPhosphoproteinsReceptor, InsulinRNA-Binding ProteinsSignal TransductionConceptsIRS 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 diabetesInsulin 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
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-1Stimulation of Protein Synthesis, Eukaryotic Translation Initiation Factor 4E Phosphorylation, and PHAS-I Phosphorylation by Insulin Requires Insulin Receptor Substrate 1 and Phosphatidylinositol 3-Kinase
Mendez R, Myers M, White M, Rhoads R. Stimulation of Protein Synthesis, Eukaryotic Translation Initiation Factor 4E Phosphorylation, and PHAS-I Phosphorylation by Insulin Requires Insulin Receptor Substrate 1 and Phosphatidylinositol 3-Kinase. Molecular And Cellular Biology 1996, 16: 2857-2864. PMID: 8649395, PMCID: PMC231278, DOI: 10.1128/mcb.16.6.2857.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCalcium-Calmodulin-Dependent Protein KinasesCarrier ProteinsCell Cycle ProteinsCell LineEukaryotic Initiation Factor-4EGRB2 Adaptor ProteinHumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsPeptide Initiation FactorsPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein BiosynthesisProtein Serine-Threonine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProteinsReceptor, InsulinRibosomal Protein S6 KinasesRNA, MessengerConceptsMitogen-activated protein kinaseProtein synthesisInsulin receptorSH-PTP2IRS-1IRS-1 variantProtein kinasePp70S6KEukaryotic translation initiation factor 4E phosphorylationMyeloid progenitor cell lineTyr residuesRecruitment of mRNAInsulin receptor substrate-1Cap-binding proteinPhosphorylation of eIF4EEndogenous insulin receptorsPHAS-I phosphorylationActivation of phosphatidylinositolReceptor substrate-1Insulin receptor substrateProgenitor cell lineGrowth-regulating proteinsCell linesGeneral protein synthesisElongation factor