2013
Nerve Growth Factor Receptor TrkA, a New Receptor in Insulin Signaling Pathway in PC12 Cells*
Geetha T, Rege S, Mathews S, Meakin S, White M, Babu J. Nerve Growth Factor Receptor TrkA, a New Receptor in Insulin Signaling Pathway in PC12 Cells*. Journal Of Biological Chemistry 2013, 288: 23807-23813. PMID: 23749991, PMCID: PMC3745327, DOI: 10.1074/jbc.m112.436279.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsEnzyme ActivationGlucoseHumansInsulinInsulin Receptor Substrate ProteinsMitogen-Activated Protein Kinase 7Molecular Sequence DataNerve Growth FactorPC12 CellsPhosphorylationPhosphotyrosineProtein BindingProto-Oncogene Proteins c-aktRatsReceptor, InsulinReceptor, trkASignal TransductionConceptsInsulin receptor substrate-1Insulin receptorPC12 cellsTrkA kinase domainTransmembrane receptor tyrosine kinaseKinase-inactive mutantInsulin Signaling PathwayReceptor substrate-1Nerve growth factor receptor TrkAReceptor tyrosine kinasesNerve growth factorActivation of AktNPXY motifKinase domainTyrosine phosphorylationSubstrate-1Regulatory loopTyrosine kinaseSignaling pathwaysGrowth factorNew receptorsReceptor TrkACellsPathwayTrkA
1997
Tyr624 and Tyr628 in Insulin Receptor Substrate-2 Mediate Its Association with the Insulin Receptor*
Sawka-Verhelle D, Baron V, Mothe I, Filloux C, White M, Van Obberghen E. Tyr624 and Tyr628 in Insulin Receptor Substrate-2 Mediate Its Association with the Insulin Receptor*. Journal Of Biological Chemistry 1997, 272: 16414-16420. PMID: 9195949, DOI: 10.1074/jbc.272.26.16414.Peer-Reviewed Original ResearchConceptsInsulin receptorIRS-2Tyrosine residuesPleckstrin homology domainPeptide competition studiesInsulin receptor substrateAmino acids 591Homology domainReceptor substrateBinding domainsRegulatory loopIRS-1Novel mechanismPosition 624ResiduesCompetition studiesReceptorsDomainIts AssociationPhosphotyrosinePhosphorylationBindsBindingRegionInteraction
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