2021
Insulin receptor substrate 1, but not IRS2, plays a dominant role in regulating pancreatic alpha cell function in mice
Takatani T, Shirakawa J, Shibue K, Gupta M, Kim H, Lu S, Hu J, White M, Kennedy R, Kulkarni R. Insulin receptor substrate 1, but not IRS2, plays a dominant role in regulating pancreatic alpha cell function in mice. Journal Of Biological Chemistry 2021, 296: 100646. PMID: 33839150, PMCID: PMC8131928, DOI: 10.1016/j.jbc.2021.100646.Peer-Reviewed Original ResearchConceptsAKT Ser/Thr kinaseInsulin receptor substrate (IRS) proteinsSer/Thr kinaseAlpha-cell functionGlobal protein translationCell functionInsulin receptor substrate-1Pancreatic alpha-cell functionDownstream target genesReceptor substrate-1Alpha cellsAlpha-cell lineGlucagon secretionSubstrate proteinsProtein translationTarget genesSubstrate-1Downstream proteinsDominant regulatorPancreatic alpha cellsMitochondrial dysfunctionCognate receptorsIRS2Normal glucose toleranceCell lines
2001
Association of Insulin Receptor Substrate 1 (IRS-1) Y895 with Grb-2 Mediates the Insulin Signaling Involved in IRS-1-Deficient Brown Adipocyte Mitogenesis
Valverde A, Mur C, Pons S, Alvarez A, White M, Kahn C, Benito M. Association of Insulin Receptor Substrate 1 (IRS-1) Y895 with Grb-2 Mediates the Insulin Signaling Involved in IRS-1-Deficient Brown Adipocyte Mitogenesis. Molecular And Cellular Biology 2001, 21: 2269-2280. PMID: 11259577, PMCID: PMC86861, DOI: 10.1128/mcb.21.7.2269-2280.2001.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseGrb-2Tyrosine phosphorylationIRS-1Brown adipocytesMAPK activationBrown adipocyte cell lineDNA synthesisActivation of MAPKWild-type IRS-1IRS-2 tyrosine phosphorylationShc tyrosine phosphorylationProtein kinase kinaseInhibition of phosphatidylinositolWild-type cell linesIRS-1 deficiencyInsulin-induced IRS-1Cell linesInsulin receptor substrate-1 (IRS-1) knockout miceAdipocyte cell lineG2/M phaseKinase kinaseMutant cellsProtein kinaseCell cycle
1998
Insulin Receptor Substrate-1 is the Predominant Signaling Molecule Activated by Insulin-like Growth Factor-I, Insulin, and Interleukin-4 in Estrogen Receptor-positive Human Breast Cancer Cells*
Jackson J, White M, Yee D. Insulin Receptor Substrate-1 is the Predominant Signaling Molecule Activated by Insulin-like Growth Factor-I, Insulin, and Interleukin-4 in Estrogen Receptor-positive Human Breast Cancer Cells*. Journal Of Biological Chemistry 1998, 273: 9994-10003. PMID: 9545345, DOI: 10.1074/jbc.273.16.9994.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesBreast NeoplasmsCalcium-Calmodulin-Dependent Protein KinasesEnzyme InhibitorsFemaleFlavonoidsHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IInterleukin-4Intracellular Signaling Peptides and ProteinsKineticsMitogen-Activated Protein Kinase KinasesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsPhosphorylationPhosphotyrosineProtein Kinase InhibitorsProtein KinasesReceptor, InsulinReceptors, EstrogenSignal TransductionTumor Cells, CulturedWortmanninConceptsIRS-1Tyrosine phosphorylationIRS-2Insulin-like growth factorBreast cancer cellsIGF-I treatmentGreater tyrosine phosphorylationInterleukin-4Substrate adaptor proteinMitogen-activated protein kinase activityCancer cellsCell linesInsulin receptor substrate-1Mitogen-activated protein kinaseP85 regulatory subunitProtein kinase activityActivation of phosphatidylinositolReceptor substrate-1Estrogen receptor-positive human breast cancer cellsGrowth factorPrimary breast tumor specimensIGF-stimulated growthAdaptor proteinRegulatory subunitT47-D breast cancer cells
1997
Janus Kinase-dependent Activation of Insulin Receptor Substrate 1 in Response to Interleukin-4, Oncostatin M, and the Interferons*
Burfoot M, Rogers N, Watling D, Smith J, Pons S, Paonessaw G, Pellegrini S, White M, Kerr I. Janus Kinase-dependent Activation of Insulin Receptor Substrate 1 in Response to Interleukin-4, Oncostatin M, and the Interferons*. Journal Of Biological Chemistry 1997, 272: 24183-24190. PMID: 9305869, DOI: 10.1074/jbc.272.39.24183.Peer-Reviewed Original ResearchConceptsInsulin receptor substrate-1Receptor substrate-1IRS-1IRS proteinsOncostatin MSubstrate-1Protein tyrosine kinasesKinase-dependent activationActivation of phosphatidylinositolJanus kinase (JAK) familyMutant cell linesHuman fibrosarcoma cell lineCell linesInsulin-like growth factor receptorHuman fibrosarcoma cellsKinase familyGrowth factor receptorFibrosarcoma cell lineIRS-2Cytokine receptorsType I interferonJAK1PhosphorylationAntiviral responseFibrosarcoma cells
1996
Stimulation of Protein Synthesis, Eukaryotic Translation Initiation Factor 4E Phosphorylation, and PHAS-I Phosphorylation by Insulin Requires Insulin Receptor Substrate 1 and Phosphatidylinositol 3-Kinase
Mendez R, Myers M, White M, Rhoads R. Stimulation of Protein Synthesis, Eukaryotic Translation Initiation Factor 4E Phosphorylation, and PHAS-I Phosphorylation by Insulin Requires Insulin Receptor Substrate 1 and Phosphatidylinositol 3-Kinase. Molecular And Cellular Biology 1996, 16: 2857-2864. PMID: 8649395, PMCID: PMC231278, DOI: 10.1128/mcb.16.6.2857.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCalcium-Calmodulin-Dependent Protein KinasesCarrier ProteinsCell Cycle ProteinsCell LineEukaryotic Initiation Factor-4EGRB2 Adaptor ProteinHumansInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsPeptide Initiation FactorsPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein BiosynthesisProtein Serine-Threonine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProteinsReceptor, InsulinRibosomal Protein S6 KinasesRNA, MessengerConceptsMitogen-activated protein kinaseProtein synthesisInsulin receptorSH-PTP2IRS-1IRS-1 variantProtein kinasePp70S6KEukaryotic translation initiation factor 4E phosphorylationMyeloid progenitor cell lineTyr residuesRecruitment of mRNAInsulin receptor substrate-1Cap-binding proteinPhosphorylation of eIF4EEndogenous insulin receptorsPHAS-I phosphorylationActivation of phosphatidylinositolReceptor substrate-1Insulin receptor substrateProgenitor cell lineGrowth-regulating proteinsCell linesGeneral protein synthesisElongation factorInsulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product.
Uddin S, Yetter A, Katzav S, Hofmann C, White M, Platanias L. Insulin-like growth factor-1 induces rapid tyrosine phosphorylation of the vav proto-oncogene product. Experimental Hematology 1996, 24: 622-7. PMID: 8605967.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineHumansInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor IIntracellular Signaling Peptides and ProteinsMicePhosphoproteinsPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-vavSignal TransductionConceptsSrc homology 2 domainVav proto-oncogene productGuanine exchange factorAntiphosphotyrosine monoclonal antibodyProto-oncogene productInsulin-like growth factor 1 receptorIGF-1 stimulationGrowth factor 1 receptorHematopoietic cell proliferationFactor 1 receptorExchange factorSH3 domainTyrosine phosphorylationPhosphorylation statusLigand bindingMediate signalsHematopoietic cellsImmunoblotting experimentsHematopoietic originCell proliferationCell linesHuman myeloma cell linesMyeloma cell linesCellsPhosphorylation