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
Characterization of selective resistance to insulin signaling in the vasculature of obese Zucker (fa/fa) rats
Jiang Z, Lin Y, Clemont A, Feener E, Hein K, Igarashi M, Yamauchi T, White M, King G. Characterization of selective resistance to insulin signaling in the vasculature of obese Zucker (fa/fa) rats. Journal Of Clinical Investigation 1999, 104: 447-457. PMID: 10449437, PMCID: PMC408521, DOI: 10.1172/jci5971.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCalcium-Calmodulin-Dependent Protein KinasesIn Vitro TechniquesInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIntracellular Signaling Peptides and ProteinsLiverMaleMicrocirculationObesityPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationRatsRats, ZuckerReceptor, InsulinRecombinant ProteinsSignal TransductionTyrosineConceptsObese ratsLean ratsObese ZuckerIRS-2-associated PIIndependent risk factorProtein levelsEuglycemic clamp studiesInsulin-resistant statesObese Zucker ratsSelective resistanceTyrosine phosphorylationVascular tissueInsulin resistanceInsulin infusionRisk factorsCardiovascular diseaseClamp studiesZucker ratsReceptor beta subunitAortaRatsInsulinInsulin receptor beta subunitERK 1/2Vivo studies
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 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 phosphorylationThe 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 Receptor Substrate-1 is the Predominant Signaling Molecule Activated by Insulin-like Growth Factor-I, Insulin, and Interleukin-4 in Estrogen Receptor-positive Human Breast Cancer Cells*
Jackson J, White M, Yee D. Insulin Receptor Substrate-1 is the Predominant Signaling Molecule Activated by Insulin-like Growth Factor-I, Insulin, and Interleukin-4 in Estrogen Receptor-positive Human Breast Cancer Cells*. Journal Of Biological Chemistry 1998, 273: 9994-10003. PMID: 9545345, DOI: 10.1074/jbc.273.16.9994.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesBreast NeoplasmsCalcium-Calmodulin-Dependent Protein KinasesEnzyme InhibitorsFemaleFlavonoidsHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IInterleukin-4Intracellular Signaling Peptides and ProteinsKineticsMitogen-Activated Protein Kinase KinasesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsPhosphorylationPhosphotyrosineProtein Kinase InhibitorsProtein KinasesReceptor, InsulinReceptors, EstrogenSignal TransductionTumor Cells, CulturedWortmanninConceptsIRS-1Tyrosine phosphorylationIRS-2Insulin-like growth factorBreast cancer cellsIGF-I treatmentGreater tyrosine phosphorylationInterleukin-4Substrate adaptor proteinMitogen-activated protein kinase activityCancer cellsCell linesInsulin receptor substrate-1Mitogen-activated protein kinaseP85 regulatory subunitProtein kinase activityActivation of phosphatidylinositolReceptor substrate-1Estrogen receptor-positive human breast cancer cellsGrowth factorPrimary breast tumor specimensIGF-stimulated growthAdaptor proteinRegulatory subunitT47-D breast cancer cells
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
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
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