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