2001
Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action*
Aguirre V, Werner E, Giraud J, Lee Y, Shoelson S, White M. Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action*. Journal Of Biological Chemistry 2001, 277: 1531-1537. PMID: 11606564, DOI: 10.1074/jbc.m101521200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnisomycinAnti-Bacterial AgentsCell LineHumansInsulinInsulin Receptor Substrate ProteinsMitogen-Activated Protein Kinase 8Mitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationRatsReceptor, InsulinRecombinant Fusion ProteinsSignal TransductionTumor Necrosis Factor-alphaTwo-Hybrid System TechniquesConceptsInsulin receptor substrate-1Phosphotyrosine-binding (PTB) domainInsulin receptorPotential phosphorylation sitesPhosphorylation of Ser307Stress-activated kinasesInsulin-stimulated kinasesReceptor substrate-1Insulin signal transductionPTB domainMAPK cascadePhosphorylation sitesMyeloid progenitor cellsSignal transductionSerine residuesCatalytic domainSerine phosphorylationDomain functionsSubstrate-1Insulin stimulationCell backgroundPhosphorylationProgenitor cellsGeneral mechanismMechanism of inhibition
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
1996
Insulin Signal Transduction and the IRS Proteins
Myers M, White M. Insulin Signal Transduction and the IRS Proteins. The Annual Review Of Pharmacology And Toxicology 1996, 36: 615-658. PMID: 8725404, DOI: 10.1146/annurev.pa.36.040196.003151.Peer-Reviewed Original ResearchConceptsIRS proteinsIntracellular tyrosine kinaseBinding of SH2Numerous intracellular signalsTyrosine phosphorylation sitesReceptor-mediated phosphorylationInsulin signal transductionPTB domainCellular physiologyPhosphorylation sitesSignal transductionIntracellular signalsExtracellular domainTyrosine kinaseCytokine receptorsBiochemical eventsInsulin receptorGlucose transportProteinPhosphorylationSignalingGrowth factorSpecific receptorsExciting moleculesPropagation of signals