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
1998
The IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action
White M, Yenush L. The IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action. Current Topics In Microbiology And Immunology 1998, 228: 179-208. PMID: 9401207, DOI: 10.1007/978-3-642-80481-6_8.Peer-Reviewed Original ResearchConceptsTyrosine phosphorylationSrc homology 2 domainTyrosine autophosphorylation sitesProtein-lipid interactionsAssembly of multicomponentSH2 proteinAutophosphorylation sitesPH domainSpecific membrane receptorsCytosolic substratesReceptor kinaseTyrosine autophosphorylationTransmembrane signalsCellular substratesCytokine receptorsActivity of receptorsMembrane receptorsEarly stepsPhosphorylationProteinKinaseGrowth factorCytokine actionReceptorsCascade
1997
Interaction of wild type and dominant-negative p55PIK regulatory subunit of phosphatidylinositol 3-kinase with insulin-like growth factor-1 signaling proteins.
Mothe I, Delahaye L, Filloux C, Pons S, White M, Van Obberghen E. Interaction of wild type and dominant-negative p55PIK regulatory subunit of phosphatidylinositol 3-kinase with insulin-like growth factor-1 signaling proteins. Endocrinology 1997, 11: 1911-23. PMID: 9415396, DOI: 10.1210/mend.11.13.0029.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportFungal ProteinsGenes, ReporterGlucoseInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IMutagenesis, Site-DirectedPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPrecipitin TestsReceptor, IGF Type 1Recombinant Fusion ProteinsSaccharomyces cerevisiaeSignal TransductionConceptsTwo-hybrid systemInsulin receptor substrate-1Receptor substrate-1Regulatory subunitSubstrate-1Src homology 2 domainInter-SH2 domainProtein-protein interactionsInhibitor of PIAmino acids 203Dominant negative mutantInsulin-stimulated glucose transportIGF-IRInsulin-like growth factor 1 receptorNH2 terminus regionDominant negative actionGrowth factor 1 receptorP110alpha catalytic subunitIGF-I stimulationSH2 domainFactor 1 receptorCatalytic subunitTyrosine phosphorylationWild typeP55PIKCalmodulin Activates Phosphatidylinositol 3-Kinase*
Joyal J, Burks D, Pons S, Matter W, Vlahos C, White M, Sacks D. Calmodulin Activates Phosphatidylinositol 3-Kinase*. Journal Of Biological Chemistry 1997, 272: 28183-28186. PMID: 9353264, DOI: 10.1074/jbc.272.45.28183.Peer-Reviewed Original ResearchConceptsSrc homology 2 domainIntact cellsPhosphorylation of phosphatidylinositolActivates PhosphatidylinositolVesicular traffickingEukaryotic cellsEffector proteinsRegulatory subunitCytoskeletal organizationUbiquitous Ca2PhosphatidylinositolIntracellular eventsNovel mechanismAffinity chromatographyGrowth factorCalmodulinCalmodulin antagonistsMultiple processesCellsCoimmunoprecipitationDirect linkPhosphorylationTraffickingSubunitsCa2The IRS-2 gene on murine chromosome 8 encodes a unique signaling adapter for insulin and cytokine action.
Sun X, Pons S, Wang L, Zhang Y, Yenush L, Burks D, Myers M, Glasheen E, Copeland N, Jenkins N, Pierce J, White M. The IRS-2 gene on murine chromosome 8 encodes a unique signaling adapter for insulin and cytokine action. Endocrinology 1997, 11: 251-62. PMID: 9013772, DOI: 10.1210/mend.11.2.9885.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBase SequenceCell DifferentiationCells, CulturedChromosome MappingChromosomesCytokinesInsulinInsulin Receptor Substrate ProteinsInterleukin-4Intracellular Signaling Peptides and ProteinsMiceMolecular Sequence DataPhosphoproteinsPhosphorylationSequence Homology, Amino AcidSignal TransductionTissue DistributionTyrosineConceptsMurine chromosome 8IRS-2IRS-1IRS-2 geneIRS proteinsExpression patternsSrc homology 2 domainChromosome 8Recombinant SH2 domainsSpecific expression patternsMurine chromosome 1Amino acid sequenceDifferential tyrosine phosphorylationMurine hematopoietic cellsDistinct phosphorylation patternsSH2 domainSignal transductionSingle exonPhosphorylation patternTyrosine phosphorylationIL-4 stimulationAcid sequenceChromosome 1Signaling adapterCytokine signaling
1996
YMXM Motifs and Signaling by an Insulin Receptor Substrate 1 Molecule without Tyrosine Phosphorylation Sites
Myers M, Zhang Y, Aldaz G, Grammer T, Glasheen E, Yenush L, Wang L, Sun X, Blenis J, Pierce J, White M. YMXM Motifs and Signaling by an Insulin Receptor Substrate 1 Molecule without Tyrosine Phosphorylation Sites. Molecular And Cellular Biology 1996, 16: 4147-4155. PMID: 8754813, PMCID: PMC231411, DOI: 10.1128/mcb.16.8.4147.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell DivisionCell LineDNA ReplicationEnzyme ActivationInsulinInsulin Receptor Substrate ProteinsMolecular Sequence DataMutagenesis, Site-DirectedPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein Serine-Threonine KinasesReceptor, InsulinRecombinant ProteinsRibosomal Protein S6 KinasesSignal TransductionStructure-Activity RelationshipConceptsTyrosine phosphorylation sitesPotential tyrosine phosphorylation sitesYMXM motifsPhosphorylation sitesIRS-1SH2 proteinTyrosine phosphorylationSrc homology 2 domainIRS-1 moleculeWild-type IRS-1Insulin receptor substrate-1Mitogen-activated protein kinaseInsulin-stimulated mitogenesisReceptor substrate-1IRS proteinsProtein kinaseMitogenic signalsMitogenic responseSubstrate-1Mitogenic sensitivityInsulin signalingInsulin stimulationPhosphotidylinositolRedundant motifsProteinInsulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product.
Uddin S, Yetter A, Katzav S, Hofmann C, White M, Platanias L. Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product. Experimental Hematology 1996, 24: 622-7. PMID: 8605967.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineHumansInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsMicePhosphoproteinsPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-vavSignal TransductionConceptsSrc homology 2 domainVav proto-oncogene productGuanine exchange factorAntiphosphotyrosine monoclonal antibodyProto-oncogene productInsulin-like growth factor 1 receptorIGF-1 stimulationGrowth factor 1 receptorHematopoietic cell proliferationFactor 1 receptorExchange factorSH3 domainTyrosine phosphorylationPhosphorylation statusLigand bindingMediate signalsHematopoietic cellsImmunoblotting experimentsHematopoietic originCell proliferationCell linesHuman myeloma cell linesMyeloma cell linesCellsPhosphorylationThe IRS-signalling system in insulin and cytokine action
White M, Marshall C. The IRS-signalling system in insulin and cytokine action. Philosophical Transactions Of The Royal Society B Biological Sciences 1996, 351: 181-189. PMID: 8650265, DOI: 10.1098/rstb.1996.0015.Peer-Reviewed Original ResearchConceptsIRS proteinsSrc homology 2 domainSH2 proteinAutophosphorylation sitesEndocytic pathwayTyrosine residuesIRS-2Cytokine receptorsRecent identificationStoichiometric constraintsMost receptorsIFN-alpha/betaAlpha/betaMultiple receptorsProteinNew insightsCytokine actionIL-13IL-4IGF-1IL-9ReceptorsIFN-gammaGrowth hormoneModular structure
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 elementsInsulin-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