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 ResearchConceptsMitogen-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 cycle
2000
IRS-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
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 signalsInsulin 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
1997
The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon-alpha receptors.
Uddin S, Fish E, Sher D, Gardziola C, Colamonici O, Kellum M, Pitha P, White M, Platanias L. The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon-alpha receptors. Blood 1997, 90: 2574-82. PMID: 9326223.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBurkitt LymphomaDNA-Binding ProteinsHematopoietic Stem CellsHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IInterferon-alphaIntracellular Signaling Peptides and ProteinsLeukemia, Myelomonocytic, AcuteLeukemia-Lymphoma, Adult T-CellMiceMultiple MyelomaNeoplasm ProteinsPhosphoproteinsReceptor, InsulinReceptor, Interferon alpha-betaReceptors, InterferonSignal TransductionSrc Homology DomainsSTAT1 Transcription FactorSTAT2 Transcription FactorSTAT3 Transcription FactorTrans-ActivatorsTumor Cells, CulturedConceptsSTAT pathwaySH2 domainHematopoietic cellsInsulin/insulin-like growth factorIRS pathwayDistinct downstream signalsTHP-1 cellsIRS-1 functionInsulin/IGFActivator of transcriptionInsulin receptor substrateDistinct signalsIFN-alphaHuman myelomonocytic cellsDocking proteinMouse myeloid cellsGrb-2P85 subunitInterferon alpha receptorSTAT-2Receptor substrateVesicular stomatitis virusSignal transducerIRS-2IRS-1
1996
The Fyn Tyrosine Kinase Binds Irs-1 and Forms a Distinct Signaling Complex during Insulin Stimulation (∗)
Sun X, Pons S, Asano T, Myers M, Glasheen E, White M. The Fyn Tyrosine Kinase Binds Irs-1 and Forms a Distinct Signaling Complex during Insulin Stimulation (∗). Journal Of Biological Chemistry 1996, 271: 10583-10587. PMID: 8631859, DOI: 10.1074/jbc.271.18.10583.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCHO CellsCricetinaeDNA PrimersEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMiceMolecular Sequence DataPhosphoproteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-fynSignal TransductionSrc Homology DomainsSubstrate SpecificityConceptsSrc homology 2Grb-2Insulin stimulationTyrosine phosphorylation sitesInsulin/IGFSH2 domainSH2 proteinSignaling ComplexHomology 2Related Src kinasesPhosphorylation sitesIR-1Src kinaseExpression libraryP59fyn kinaseTyrosine residuesP59fynInsulin receptorIR proteinProteinSpecific associationComplexesKinaseReceptorsP85