2005
Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: Role of IRS phosphorylation
Zhang Q, Carter E, Ma B, White M, Fischman A, Tompkins R. Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: Role of IRS phosphorylation. Life Sciences 2005, 77: 3068-3077. PMID: 15982669, DOI: 10.1016/j.lfs.2005.02.034.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBurnsDisease Models, AnimalEnzyme ActivationHindlimbInsulin Receptor Substrate ProteinsInsulin ResistanceJNK Mitogen-Activated Protein KinasesMaleMAP Kinase Kinase 4MiceMitogen-Activated Protein Kinase KinasesMuscle, SkeletalPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptor, InsulinSignal TransductionConceptsInsulin receptor substrate-1Burn-induced insulin resistanceAkt kinase activityIRS-1 proteinSAPK/JNKSerine 307Kinase activitySkeletal muscleReceptor substrate-1Murine skeletal muscleHind limb skeletal muscleStress kinasesKey proteinsSubstrate-1Biochemical basisPhosphorylationIRS phosphorylationKinase enzymeProteinEnzyme activityJNKLimb skeletal muscleProtein contentInsulin resistanceKinaseInsulin Receptor Substrate 2 Plays Diverse Cell-specific Roles in the Regulation of Glucose Transport*
Sadagurski M, Weingarten G, Rhodes C, White M, Wertheimer E. Insulin Receptor Substrate 2 Plays Diverse Cell-specific Roles in the Regulation of Glucose Transport*. Journal Of Biological Chemistry 2005, 280: 14536-14544. PMID: 15705592, DOI: 10.1074/jbc.m410227200.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsBiological TransportDeoxyglucoseEpidermisFibroblastsGenotypeGlucoseHomozygoteImmunoblottingImmunoprecipitationInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsKeratinocytesMiceMice, KnockoutPhosphatidylinositol 3-KinasesPhosphoproteinsSkinThymidineTime FactorsConceptsIRS-2Glucose transportInsulin receptor substrate-2 proteinInsulin-induced glucose transportInsulin receptor substrate 2Insulin-stimulated glucose transportIRS-1 proteinCell specific associationIRS-2 proteinClassical insulin target tissuesCell-specific mannerSkin epidermal keratinocytesIRS-PICell-specific rolePositive regulatorInsulin target tissuesCell physiologyDermal fibroblastsKO cellsEpidermal keratinocytesAkt activationPhosphatidylinositolSubstrate 2Insulin receptorProtein
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
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 levelsActivation of the phosphatidylinositol 3-kinase serine kinase by IFN-alpha.
Uddin S, Fish E, Sher D, Gardziola C, White M, Platanias L. Activation of the phosphatidylinositol 3-kinase serine kinase by IFN-alpha. The Journal Of Immunology 1997, 158: 2390-7. PMID: 9036989, DOI: 10.4049/jimmunol.158.5.2390.Peer-Reviewed Original ResearchConceptsSerine kinaseTreatment of cellsIRS-1Kinase assaysSerine kinase activityDual-specificity enzymeP85 regulatory subunitReceptor-generated signalsIRS-1 proteinJak-1 kinasesIFN-alpha-induced activationProtein associatesP85 subunitPhosphoaminoacid analysisRegulatory subunitSerine residuesSerine phosphorylationTyrosine phosphorylationTyk-2STAT-2MAP kinaseKinase activityPretreatment of cellsInhibitor wortmanninPhosphatidylinositol
1993
Insulin-Stimulated Oocyte Maturation Requires Insulin Receptor Substrate 1 and Interaction with the SH2 Domains of Phosphatidylinositol 3-Kinase
Chuang L, Myers M, Backer J, Shoelson S, White M, Birnbaum M, Kahin C. Insulin-Stimulated Oocyte Maturation Requires Insulin Receptor Substrate 1 and Interaction with the SH2 Domains of Phosphatidylinositol 3-Kinase. Molecular And Cellular Biology 1993, 13: 6653-6660. DOI: 10.1128/mcb.13.11.6653-6660.1993.Peer-Reviewed Original ResearchSrc homology 2 domainSrc homology 2PtdIns 3-kinaseSrc homology 2 domains of p85Glutathione S-transferase fusion proteinS-transferase fusion proteinDomains of p85IRS-1Ras-GAPP85 subunit of PtdIns 3-kinaseFusion proteinActivation of PtdIns 3-kinasePtdIns 3-kinase activitySubstrate 1Phosphorylation of IRS-1IRS-1 associationInsulin receptor substrate 1Insulin-stimulated phosphatidylinositolIRS-1 proteinPhosphorylated IRS-1Progesterone-induced oocyte maturationP85 subunitOocyte maturationInsulin signalingResponse to hormonal stimulation