1998
Interaction of Insulin Receptor Substrate-1 (IRS-1) with Phosphatidylinositol 3-Kinase: Effect of Substitution of Serine for Alanine in Potential IRS-1 Serine Phosphorylation Sites
Delahaye L, Mothe-Satney I, Myers M, White M, Van Obberghen E. Interaction of Insulin Receptor Substrate-1 (IRS-1) with Phosphatidylinositol 3-Kinase: Effect of Substitution of Serine for Alanine in Potential IRS-1 Serine Phosphorylation Sites. Endocrinology 1998, 139: 4911-4919. DOI: 10.1210/en.139.12.4911.Peer-Reviewed Original ResearchInsulin receptor substrate-1Protein kinase B activationSerine phosphorylation sitesPI 3-kinaseRegulatory subunitPotential binding sitesPhosphorylation sitesTyrosine phosphorylationRegulatory subunit of PI 3-kinasePI 3-kinase regulatory subunitSubunit of PI 3-kinaseTyrosine phosphorylation of insulin receptor substrate-1Interaction of insulin receptor substrate-1Phosphorylation of insulin receptor substrate-1Yeast two-hybrid systemInsulin-stimulated PI 3-kinase activityWild-type IRS-1Potential serine phosphorylation sitesLevel of insulin receptor substrate-1PI 3-kinase activityRegulatory subunit of phosphatidylinositolPhosphorylated insulin receptor substrate-1Two-hybrid systemBinding sitesSubstitution of serineInteraction of insulin receptor substrate-1 (IRS-1) with phosphatidylinositol 3-kinase: effect of substitution of serine for alanine in potential IRS-1 serine phosphorylation sites.
Delahaye L, Mothe-Satney I, Myers M, White M, Van Obberghen E. Interaction of insulin receptor substrate-1 (IRS-1) with phosphatidylinositol 3-kinase: effect of substitution of serine for alanine in potential IRS-1 serine phosphorylation sites. Endocrinology 1998, 139: 4911-9. PMID: 9832428, DOI: 10.1210/endo.139.12.6379.Peer-Reviewed Original ResearchConceptsInsulin receptor substrate-1Protein kinase B activitySerine phosphorylation sitesRegulatory subunitReceptor substrate-1Phosphorylation sitesPotential binding sitesTyrosine phosphorylationSubstrate-1Potential tyrosine phosphorylation sitesIRS-1 interactsPotential serine phosphorylation sitesWild-type IRS-1Two-hybrid systemTyrosine phosphorylation sitesInsulin-stimulated phosphatidylinositolPhosphorylate IRS-1P85alpha regulatory subunitBinding sitesYeast kinasesThreonine phosphorylationSerine mutantsYXXM motifsB activityP85alphaIRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins*
Burks D, Wang J, Towery H, Ishibashi O, Lowe D, Riedel H, White M. IRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins*. Journal Of Biological Chemistry 1998, 273: 31061-31067. PMID: 9813005, DOI: 10.1074/jbc.273.47.31061.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acids, DicarboxylicATP-Dependent ProteasesBinding SitesBlood ProteinsHeat-Shock ProteinsInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsLigandsMolecular Sequence DataOligopeptidesPeptide FragmentsPhosphoproteinsProtein BindingRecombinant ProteinsRNA-Binding ProteinsSequence Homology, Amino AcidSerine EndopeptidasesConceptsPH domainAcidic motifIRS-2IRS-1IRS proteinsLon proteaseInsulin-stimulated tyrosine phosphorylationTwo-hybrid systemBinding of nucleolinPleckstrin homologyPhospholipase CgammaMembrane proteinsTyrosine phosphorylationNucleolinPeptide motifsMembrane receptorsInsulin receptorSpecific functionsProteinMotifInsulin actionProteaseSynthetic peptidesBindingDomain
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 typeP55PIK
1996
Insulin Receptor Substrate-2 Binds to the Insulin Receptor through Its Phosphotyrosine-binding Domain and through a Newly Identified Domain Comprising Amino Acids 591–786 (∗)
Sawka-Verhelle D, Tartare-Deckert S, White M, Van Obberghen E. Insulin Receptor Substrate-2 Binds to the Insulin Receptor through Its Phosphotyrosine-binding Domain and through a Newly Identified Domain Comprising Amino Acids 591–786 (∗). Journal Of Biological Chemistry 1996, 271: 5980-5983. PMID: 8626379, DOI: 10.1074/jbc.271.11.5980.Peer-Reviewed Original ResearchConceptsTwo-hybrid systemIRS-2IRS-1Insulin receptorNPEY motifNPXY motifPhosphotyrosine-binding (PTB) domainPleckstrin homology domainTyrosine phosphorylation sitesActivated insulin receptorInsulin receptor kinaseIRS-2 phosphorylationReceptor tyrosine kinase activityTyrosine kinase activityAmino acids 591IRS proteinsHomology domainPhosphorylation sitesInteraction domainReceptor kinaseCytoplasmic portionBinding domainsKinase activityRegulatory loopNH2 terminus