2016
Serine 302 Phosphorylation of Mouse Insulin Receptor Substrate 1 (IRS1) Is Dispensable for Normal Insulin Signaling and Feedback Regulation by Hepatic S6 Kinase*
Copps K, Hançer N, Qiu W, White M. Serine 302 Phosphorylation of Mouse Insulin Receptor Substrate 1 (IRS1) Is Dispensable for Normal Insulin Signaling and Feedback Regulation by Hepatic S6 Kinase*. Journal Of Biological Chemistry 2016, 291: 8602-8617. PMID: 26846849, PMCID: PMC4861431, DOI: 10.1074/jbc.m116.714915.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsCHO CellsCricetinaeCricetulusGene DeletionGlucose IntoleranceInsulinInsulin Receptor Substrate ProteinsLiverMechanistic Target of Rapamycin Complex 1MiceMice, TransgenicMultiprotein ComplexesMutation, MissensePhosphatidylinositol 3-KinasesPhosphorylationProto-Oncogene Proteins c-aktRibosomal Protein S6 KinasesSerineSignal TransductionTOR Serine-Threonine KinasesTuberous Sclerosis Complex 1 ProteinTumor Suppressor ProteinsConceptsInsulin receptor substrate-1Receptor substrate-1PI3K associationS6 kinaseSubstrate-1Insulin-stimulated Akt activityAkt phosphorylationK associationRapamycin complex 1S6K signalingInsulin-stimulated IRS1 tyrosine phosphorylationSer-302IRS1 tyrosine phosphorylationMTORC1 inhibitor rapamycinRibosomal S6 proteinTsc1 deletionFeedback phosphorylationIntracellular amino acidsInsulin sensitivityTyrosine phosphorylationAlanine mutationsS6 proteinS6KAkt activityInsulin signaling
2009
Targeted Disruption of ROCK1 Causes Insulin Resistance in Vivo *
Lee D, Shi J, Jeoung N, Kim M, Zabolotny J, Lee S, White M, Wei L, Kim Y. Targeted Disruption of ROCK1 Causes Insulin Resistance in Vivo *. Journal Of Biological Chemistry 2009, 284: 11776-11780. PMID: 19276091, PMCID: PMC2673246, DOI: 10.1074/jbc.c900014200.Peer-Reviewed Original ResearchMeSH KeywordsAdiposityAnimalsDiabetes Mellitus, Type 2GlucoseGTPase-Activating ProteinsInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceMiceMice, KnockoutObesityPhosphatidylinositol 3-KinasesPhosphorylationProto-Oncogene Proteins c-aktRho-Associated KinasesRibosomal Protein S6 KinasesSignal TransductionConceptsIRS-1Skeletal muscleWhole-body glucose homeostasisInsulin resistanceBody glucose homeostasisCultured cell linesPhosphorylation of AktPhospho-tyrosinesGlucose homeostasisROCK1-deficient miceSerine phosphorylationNovel regulatorTyrosine phosphorylationS6KRho kinase isoformsInsulin sensitivityPhysiological roleGene ablationAbility of insulinInsulin receptorTargeted disruptionPhosphorylationNormal glucose homeostasisGlucose-induced insulin secretionROCK1
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
1998
The Pleckstrin Homology and Phosphotyrosine Binding Domains of Insulin Receptor Substrate 1 Mediate Inhibition of Apoptosis by Insulin
Yenush L, Zanella C, Uchida T, Bernal D, White M. The Pleckstrin Homology and Phosphotyrosine Binding Domains of Insulin Receptor Substrate 1 Mediate Inhibition of Apoptosis by Insulin. Molecular And Cellular Biology 1998, 18: 6784-6794. PMID: 9774692, PMCID: PMC109262, DOI: 10.1128/mcb.18.11.6784.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell LineCell SurvivalChromonesDNAInsulinInsulin Receptor Substrate ProteinsInterleukin-3MorpholinesPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotyrosineReceptor, InsulinRecombinant Fusion ProteinsRibosomal Protein S6 KinasesConceptsPhosphotyrosine-binding (PTB) domainTyrosine phosphorylation sitesPleckstrin homologyIRS-1 proteinIRS-1Phosphorylation sitesInsulin receptorBinding domainsInsulin receptor substrate (IRS) proteinsReceptor-mediated tyrosine phosphorylationInsulin stimulationChimeric insulin receptorsPKB/AktIL-3 withdrawalIRS proteinsSubstrate proteinsPTB domainKinase cascadeMediated phosphorylationInhibition of apoptosisMyeloid progenitor cellsDiverse biological effectsPhosphatidylinositol 3Protein kinaseTyrosine phosphorylation
1997
Requirement 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 expression
1996
The Pleckstrin Homology Domain Is the Principle Link between the Insulin Receptor and IRS-1*
Yenush L, Makati K, Smith-Hall J, Ishibashi O, Myers M, White M. The Pleckstrin Homology Domain Is the Principle Link between the Insulin Receptor and IRS-1*. Journal Of Biological Chemistry 1996, 271: 24300-24306. PMID: 8798677, DOI: 10.1074/jbc.271.39.24300.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesBlood ProteinsCell LineInsulin Receptor Substrate ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein BindingProtein Serine-Threonine KinasesReceptor, InsulinRecombinant ProteinsRibosomal Protein S6 KinasesYMXM 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 motifsProteinStimulation 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 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