2009
Insulin-Like Growth Factor 2 and the Insulin Receptor, But Not Insulin, Regulate Fetal Hepatic Glycogen Synthesis
Liang L, Guo W, Esquiliano D, Asai M, Rodriguez S, Giraud J, Kushner J, White M, Lopez M. Insulin-Like Growth Factor 2 and the Insulin Receptor, But Not Insulin, Regulate Fetal Hepatic Glycogen Synthesis. Endocrinology 2009, 151: 741-747. PMID: 20032056, PMCID: PMC2817628, DOI: 10.1210/en.2009-0705.Peer-Reviewed Original ResearchConceptsGlycogen synthesisInsulin receptorFetal liverInsulin receptor substrate 2Insulin-like growth factor 2Knockout mouse strainIR-A isoformGlycogen synthaseMajor regulatorGrowth factor 2Akt proteinSubstrate 2Insulin receptor isoformsGlycogen metabolismIgf2 deficiencyPDX-1Factor 2Receptor isoformsHepatic glycogen synthesisHepatic glycogen metabolismINSRIGF2Fetal hepatocytesIsoformsMouse strains
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 associationComplexesKinaseReceptorsP85Insulin 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