1999
Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2 †
Chung H, Nairn A, Murata K, Brautigan D. Mutation of Tyr307 and Leu309 in the Protein Phosphatase 2A Catalytic Subunit Favors Association with the α4 Subunit Which Promotes Dephosphorylation of Elongation Factor-2 †. Biochemistry 1999, 38: 10371-10376. PMID: 10441131, DOI: 10.1021/bi990902g.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnion Exchange ResinsBacterial ProteinsCatalytic DomainChromatography, Ion ExchangeCOS CellsHemagglutininsLectinsLeucineMutagenesis, Site-DirectedOligopeptidesPeptide Elongation Factor 2Peptide Elongation FactorsPeptidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPrecipitin TestsProtein Phosphatase 2Resins, SyntheticTransfectionTyrosineConceptsAlpha 4 proteinElongation factor 2AC dimerC subunitSpecific intracellular substratesProtein phosphatase 2ASites of phosphorylationAbc trimerCOS-7 cellsFactor 2B subunitC-terminal residuesTOR proteinsPhosphatase 2ANovel subunitCatalytic subunitTransient overexpressionSubstrate specificityCellular locationIntracellular substratesTransient expressionP70S6 kinaseSingle mutationProtein synthesisSubunits
1997
N-methyl-d-aspartate receptor activation and visual activity induce elongation factor-2 phosphorylation in amphibian tecta: A role for N-methyl-d-aspartate receptors in controlling protein synthesis
Scheetz A, Nairn A, Constantine-Paton M. N-methyl-d-aspartate receptor activation and visual activity induce elongation factor-2 phosphorylation in amphibian tecta: A role for N-methyl-d-aspartate receptors in controlling protein synthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 14770-14775. PMID: 9405688, PMCID: PMC25112, DOI: 10.1073/pnas.94.26.14770.Peer-Reviewed Original ResearchConceptsEukaryotic translation elongation factor 2EEF2 phosphorylationProtein synthesisTranslation elongation factor 2Elongation factor 2 phosphorylationProtein synthetic machinerySubset of proteinsFactor 2 phosphorylationElongation factor 2Synaptic plasticityNMDAR activationNumerous transcriptsProtein translationReceptor activationNew proteinsTranscriptional alterationsSynthetic machineryPhosphorylationN-methyl-D-aspartate (NMDA) receptor activationDendritic localizationN-methyl-D-aspartate receptorsProtein expressionFactor 2Aspartate receptor activationProteinGlutamate-Dependent Phosphorylation of Elongation Factor-2 and Inhibition of Protein Synthesis in Neurons
Marin P, Nastiuk K, Daniel N, Girault J, Czernik A, Glowinski J, Nairn A, Prémont J. Glutamate-Dependent Phosphorylation of Elongation Factor-2 and Inhibition of Protein Synthesis in Neurons. Journal Of Neuroscience 1997, 17: 3445-3454. PMID: 9133370, PMCID: PMC6573691, DOI: 10.1523/jneurosci.17-10-03445.1997.Peer-Reviewed Original ResearchMeSH Keywords6-Cyano-7-nitroquinoxaline-2,3-dioneAnimalsAntibody SpecificityCalciumCell SurvivalCells, CulturedCerebral CortexDizocilpine MaleateExcitatory Amino Acid AntagonistsGlutamic AcidMiceNerve Tissue ProteinsNeuronsNeurotoxinsPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationProtein BiosynthesisProtein Synthesis InhibitorsReceptors, AMPAReceptors, N-Methyl-D-AspartateConceptsNeuronal deathEukaryotic elongation factor 2Factor 2Cortical neuronsElongation factor 2Glutamate receptorsProtective effectLong-term effectsProtein synthesisPersistent inhibitionPharmacological analysisPharmacological inhibitionCytosolic Ca2Phosphorylation state-specific antibodiesNeuronsNMDAGlutamateInhibitionProtein translationDeathPhosphorylationClose correlationTransient phosphorylationCa2Excitotoxicity
1996
Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*
Marino M, Dunbar J, Wu L, Ngaiza J, Han H, Guo D, Matsushita M, Nairn A, Zhang Y, Kolesnick R, Jaffe E, Donner D. Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine*. Journal Of Biological Chemistry 1996, 271: 28624-28629. PMID: 8910494, DOI: 10.1074/jbc.271.45.28624.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAnimalsCattleEndothelium, VascularEnzyme InhibitorsEukaryotic Initiation Factor-4EHistaminePeptide Elongation Factor 2Peptide Elongation FactorsPeptide Initiation FactorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafSignal TransductionTumor Necrosis Factor-alphaConceptsBovine aortic endothelial cellsElongation factor 2Distinct signal transduction cascadesEukaryotic initiation factor 4ETNF signal transduction pathwayEF-2 phosphorylationC-Jun N-terminal kinaseSignal transduction cascadeInitiation factor 4EProtein kinase activitySignal transduction pathwaysEndothelial cellsN-terminal kinaseTNF actionPhosphorylation cascadeEIF-4ESignal transductionTransduction cascadeTransduction pathwaysResponse of BAECsJun-B expressionKinase activityProtein synthesisPhosphorylationCell types
1994
Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins.
Terada N, Patel H, Takase K, Kohno K, Nairn A, Gelfand E. Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 11477-11481. PMID: 7972087, PMCID: PMC45254, DOI: 10.1073/pnas.91.24.11477.Peer-Reviewed Original ResearchConceptsRibosomal proteinsElongation factorProtein synthesisRibosomal protein mRNAsRibosomal protein synthesisTranslation of mRNAsP70 S6 kinaseRibosomal S6 proteinElongation factor 2Higher eukaryotesNonribosomal proteinsPolysomal associationRate of biosynthesisTranslational regulationMammalian cellsMRNA translationS6 kinaseAddition of rapamycinS6 proteinSubsequent phosphorylationEEF-2Translational levelImmunosuppressant rapamycinQuiescent cellsSelective proteinsRole of elongation factor 2 in regulating peptide-chain elongation in the heart
Vary T, Nairn A, Lynch C. Role of elongation factor 2 in regulating peptide-chain elongation in the heart. American Journal Of Physiology 1994, 266: e628-e634. PMID: 7513958, DOI: 10.1152/ajpendo.1994.266.4.e628.Peer-Reviewed Original ResearchConceptsDiabetic ratsEF-2 contentFactor 2Protein synthesisInsulin therapyIncrease of RNADecreased translational efficiencyElongation factor 2RatsDiabetesCardiac muscleImpaired rateDecreased rateProgressive decreaseHeartInhibitionMolecular mechanismsRNA contentPeptide chain elongationH durationTherapyInsulinDecrease
1993
Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas
Mitsui K, Brady M, Palfrey H, Nairn A. Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas. Journal Of Biological Chemistry 1993, 268: 13422-13433. PMID: 8514778, DOI: 10.1016/s0021-9258(19)38667-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCattleChromatography, GelElectrophoresis, Polyacrylamide GelElongation Factor 2 KinaseHeat-Shock ProteinsMolecular Sequence DataPancreasPeptide Elongation Factor 2Peptide Elongation FactorsPeptide MappingPhosphoproteinsPhosphorylationProtein KinasesRabbitsRatsReticulocytesSubstrate SpecificityConceptsEukaryotic elongation factor 2CaM kinase IIICalmodulin-dependent protein kinase IIIProtein kinase IIIKinase IIIProtein kinaseRabbit reticulocytesCAMP-dependent protein kinaseYeast EF-2Heat shock protein Hsp90Novel protein kinaseElongation factor 2Amino acid sequencingPhosphopeptide mappingSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisProtein Hsp90Catalytic subunitSulfate-polyacrylamide gel electrophoresisSeryl residuesMajor polypeptidesSubstrate ATPHsp90Factor 2Gel electrophoresisPhosphorylation of elongation factor 2 in normal and malignant rat glial cells.
Bagaglio DM, Cheng EH, Gorelick FS, Mitsui K, Nairn AC, Hait WN. Phosphorylation of elongation factor 2 in normal and malignant rat glial cells. Cancer Research 1993, 53: 2260-4. PMID: 8485712.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCell DivisionCells, CulturedElongation Factor 2 KinaseGliomaMaleNeurogliaPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationPrecipitin TestsProtein KinasesRatsRats, Sprague-DawleyTrifluoperazineTumor Cells, CulturedConceptsRat brain white matterNormal glial tissueGlial tissueGlioma cellsC6 cellsC6 rat glioma cellsCaM kinase IIIRat glial cellsFactor 2Rat glioma cellsBrain white matterNormal gliaElongation factor 2Glial cellsRat brainWhite matterTumor tissueBasal levelsIII activityCellular proliferationTissueDependent proteinsCellsEndogenous substratesHomogenates
1992
Increased phosphorylation of elongation factor 2 in Alzheimer's disease
Johnson G, Gotlib J, Haroutunian V, Bierer L, Nairn A, Merril C, Wallace W. Increased phosphorylation of elongation factor 2 in Alzheimer's disease. Brain Research 1992, 15: 319-326. PMID: 1331687, DOI: 10.1016/0169-328x(92)90124-t.Peer-Reviewed Original ResearchConceptsDisease brainAlzheimer's diseaseAlzheimer's disease brainFactor 2AD homogenatesAD tissueElongation factor 2Brain homogenatesSame brainDiseaseVariant isoformsProtein synthesisPhosphorylated formInhibits protein synthesisBrainUnaffected areasHomogenatesAcidic isoformsPhosphorylationGene expressionEF-2Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini
Hincke M, Nairn A. Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini. Biochemical Journal 1992, 282: 877-882. PMID: 1372803, PMCID: PMC1130869, DOI: 10.1042/bj2820877.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Two-dimensional PAGECalmodulin-dependent phosphorylationRapid phosphorylationParotid acinar cellsMolecular mechanismsRat parotid cellsPhosphorylationPhorbol esterStimulation of secretionProteinParotid cellsAcinar cellsRat parotid aciniParotid aciniSpecific antiseraCellsCa2ImmunoprecipitationExtracellular Ca2SecretionStimulationInhibition
1990
Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells.
Demolle D, Lecomte M, Boutherin-Falson O, Cragoe E, Nairn A, Boeynaems J. Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells. Molecular Pharmacology 1990, 37: 827-32. PMID: 2359404.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Rabbit reticulocyte lysateCell-free systemBovine aortic endothelial cellsDependent phosphorylationReticulocyte lysateEndothelial cellsAmiloride analoguesPhosphorylationSimilar MrCytosolic pHVascular endothelial cellsProteinAnalogues of amilorideAortic endothelial cellsPotent inhibitorInhibitory effectAntiportCellsEIPAAmilorideATPLysatesRole of Ca2+/calmodulin-dependent protein phosphorylation in signal transduction.
Nairn A. Role of Ca2+/calmodulin-dependent protein phosphorylation in signal transduction. 1990, 24: 202-5. PMID: 1976329.Peer-Reviewed Original Research
1989
Insulin rapidly induces the biosynthesis of elongation factor 2
Levenson R, Nairn A, Blackshear P. Insulin rapidly induces the biosynthesis of elongation factor 2. Journal Of Biological Chemistry 1989, 264: 11904-11911. PMID: 2663845, DOI: 10.1016/s0021-9258(18)80152-1.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCells, CulturedDactinomycinDrug SynergismElectrophoresis, Gel, Two-DimensionalHumansInsulinPeptide Elongation Factor 2Peptide Elongation FactorsPrecipitin TestsConceptsElongation factor 2EF-2Overall protein synthesisProtein synthesisProtein translation apparatusEukaryotic elongation factor 2Two-dimensional gel electrophoresisHuman insulin receptorNIH 3T3 cellsFactor 2Translation apparatusMature speciesMRNA translationActinomycin D. ThusRNA transcription inhibitorSuch proteinsIndividual proteinsInsulin inductionPreferential expressionPrecursor formInsulin receptorSerum deprivationProteinGel autoradiographsGel electrophoresisThrombin and Histamine Stimulate the Phosphorylation of Elongation Factor 2 in Human Umbilical Vein Endothelial Cells
Mackie K, Nairn A, Hampel G, Lam G, Jaffe E. Thrombin and Histamine Stimulate the Phosphorylation of Elongation Factor 2 in Human Umbilical Vein Endothelial Cells. Journal Of Biological Chemistry 1989, 264: 1748-1753. PMID: 2536373, DOI: 10.1016/s0021-9258(18)94250-x.Peer-Reviewed Original ResearchConceptsHuman umbilical vein endothelial cellsElongation factor 2EF-2Calmodulin-dependent protein kinase IIIUmbilical vein endothelial cellsProtein synthesisVein endothelial cellsProtein kinase IIIPhosphoamino acid analysisFactor 2Kinase IIICell protein synthesisProtein phosphorylationCultured human umbilical vein endothelial cellsEndothelial cellsPeptidyl-tRNAPhosphorylationBiochemical studiesRapid transient increaseAcid analysisPhorbol dibutyrateIncubation of HUVECsIntracellular calcium levelsProteinEffect of thrombin
1987
Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2.
Nairn A, Palfrey H. Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. Journal Of Biological Chemistry 1987, 262: 17299-17303. PMID: 3693353, DOI: 10.1016/s0021-9258(18)45377-x.Peer-Reviewed Original ResearchConceptsProtein kinase IIIElongation factor 2Kinase IIIMammalian cellsThreonine residuesCalmodulin-dependent protein kinase IIIDependent protein kinase IIIPhosphorylated EF-2Endogenous GTPase activityAmino acid sequencingSpecies of MrFactor 2Inhibits protein synthesisTryptic phosphopeptidesGTPase activityNucleic acid sequencingCytoplasmic localizationMajor substrateN-terminalPeptidyl-tRNATerminal sequenceSalt-washed ribosomesProtein synthesisEF-1Thr-Asp