2004
Islet-Sparing Effects of Protein Tyrosine Phosphatase-1b Deficiency Delays Onset of Diabetes in IRS2 Knockout Mice
Kushner J, Haj F, Klaman L, Dow M, Kahn B, Neel B, White M. Islet-Sparing Effects of Protein Tyrosine Phosphatase-1b Deficiency Delays Onset of Diabetes in IRS2 Knockout Mice. Diabetes 2004, 53: 61-66. PMID: 14693698, DOI: 10.2337/diabetes.53.1.61.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlood GlucoseCrosses, GeneticDiabetes Mellitus, Type 1Glucose Tolerance TestInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsIslets of LangerhansKineticsLeptinMaleMiceMice, KnockoutModels, AnimalPhosphoproteinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesSignal TransductionConceptsPeripheral insulin sensitivityBeta-cell areaBeta-cell functionInsulin sensitivityPancreatic beta cell areaPancreatic beta-cell functionDecreased insulin requirementIrs2 knockout miceBeta cell homeostasisMonths of ageInsulin requirementsPeripheral actionsGlucose toleranceGlucose homeostasisKnockout miceDelay onsetMiceInsulin receptorPTP1B deficiencyDiabetesReceptor complexIRS2Novel roleInsulinDownstream targets
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
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 PTP1B
1999
Differential 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
The 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 signals
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 factor