1998
The IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Molecular And Cellular Biochemistry 1998, 182: 3-11. PMID: 9609109, DOI: 10.1023/a:1006806722619.Peer-Reviewed Original ResearchConceptsIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetesThe IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Developments In Molecular And Cellular Biochemistry 1998, 3-11. DOI: 10.1007/978-1-4615-5647-3_1.Peer-Reviewed Original ResearchIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetes
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
1993
Pleiotropic Insulin Signals are Engaged by Multisite Phosphorylation of IRS-1
Sun X, Crimmins D, Myers M, Miralpeix M, White M. Pleiotropic Insulin Signals are Engaged by Multisite Phosphorylation of IRS-1. Molecular And Cellular Biology 1993, 13: 7418-7428. DOI: 10.1128/mcb.13.12.7418-7428.1993.Peer-Reviewed Original ResearchSrc homology 2IRS-1SH2 domainInsulin signalingPotential tyrosine phosphorylation sitesTyrosine residuesSrc homology 2 domainSrc homology 2 proteinAmino-terminal SH2 domainInsulin stimulationPhosphorylation of tyrosine residuesTyrosine phosphorylation sitesMultisite docking proteinInsulin signal transmissionInsulin receptor substrateInsulin receptor kinaseInsulin-stimulated phosphorylationDownstream regulatory elementsPurified insulin receptorYMXM motifsActivating insulin receptor kinaseDocking proteinMultisite phosphorylationPhosphorylation sitesRegulatory elements