2006
2‐Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor‐2 by distinct mechanisms
Maus M, Torrens Y, Gauchy C, Bretin S, Nairn A, Glowinski J, Premont J. 2‐Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor‐2 by distinct mechanisms. Journal Of Neurochemistry 2006, 96: 815-824. PMID: 16405506, DOI: 10.1111/j.1471-4159.2005.03601.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimetabolitesBlotting, WesternCalciumCarbonyl Cyanide m-Chlorophenyl HydrazoneCells, CulturedCerebral CortexDeoxyglucoseDose-Response Relationship, DrugDrug InteractionsEmbryo, MammalianEnzyme InhibitorsExcitatory Amino Acid AgonistsIonophoresLeucineMiceModels, BiologicalNeuronsN-MethylaspartateOligomycinsPeptide Elongation Factor 2PhosphorylationProtein KinasesProtein Synthesis InhibitorsPyruvic AcidSodium AzideTime FactorsTOR Serine-Threonine KinasesTritiumConceptsCortical neuronsExcitatory amino acid releaseImine hydrogen maleateNMDA receptor antagonistAMP kinaseAmino acid releaseNeuronal protein synthesisCytosolic free Ca2Protein synthesisCerebral ischaemiaReceptor antagonistBrain damageNeuronal metabolismMetabolic impairmentNMDADistinct mechanismsCytosolic Ca2NeuronsMetabolic deprivationAcid releaseSecondary releaseProtein synthesis inhibitionSynthesis inhibitionElongation factor eEF-2ATP levels
2001
Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*
Bibb J, Nishi A, O'Callaghan J, Ule J, Lan M, Snyder G, Horiuchi A, Saito T, Hisanaga S, Czernik A, Nairn A, Greengard P. Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*. Journal Of Biological Chemistry 2001, 276: 14490-14497. PMID: 11278334, DOI: 10.1074/jbc.m007197200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBrainCalcineurinCarrier ProteinsCDC2 Protein KinaseCyclic AMPCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesGlutamic AcidIntracellular Signaling Peptides and ProteinsKineticsMiceMice, Inbred C57BLMutagenesis, Site-DirectedN-MethylaspartatePhosphoprotein PhosphatasesPhosphorylationProlineProtein Phosphatase 1RabbitsRatsRecombinant ProteinsRNA-Binding ProteinsSerineTime FactorsConceptsProtein phosphatase inhibitor-1Protein phosphatase 1Phosphatase inhibitor-1Ser-67Protein kinasePhosphatase 1CAMP-dependent protein kinase resultsSelective protein kinase inhibitorsCAMP-dependent protein kinaseProtein phosphatase 2AProline-directed kinasesMitogen-activated protein kinaseInhibitor-1Protein kinase resultsSignal transduction eventsPhosphorylation state-specific antibodiesCAMP-dependent protein kinase activationState of phosphorylationProtein kinase inhibitorsProtein kinase activationPhosphatase 2AThr-35Protein phosphatasePhosphorylation sitesGlutamate-dependent regulation
2000
NMDA receptor-mediated control of protein synthesis at developing synapses
Scheetz A, Nairn A, Constantine-Paton M. NMDA receptor-mediated control of protein synthesis at developing synapses. Nature Neuroscience 2000, 3: 211-216. PMID: 10700251, DOI: 10.1038/72915.Peer-Reviewed Original ResearchMeSH Keywords2-Amino-5-phosphonovalerateAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCycloheximideElectrophoresis, Gel, Two-DimensionalGlutamic AcidIsoelectric PointMolecular WeightN-MethylaspartatePeptide Elongation Factor 2PhosphorylationPrecipitin TestsProtein BiosynthesisProteinsRatsReceptors, N-Methyl-D-AspartateRetinal Ganglion CellsSuperior ColliculiSynapsesSynaptosomesTime FactorsConceptsNMDAR activationReceptor activationN-methyl-D-aspartate (NMDA) receptor activationActivity-dependent synaptic changesEukaryotic elongation factor 2Receptor-mediated controlSynaptic protein synthesisEEF2 phosphorylationProtein synthesisSuperior colliculiYoung ratsDependent kinase IISynaptic changesLow dosesTotal protein synthesisII synthesisFactor 2Overall protein synthesisActivationElongation factor 2Kinase IIPhosphorylation
1999
Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue
Nishimoto G, Zelenina M, Li D, Yasui M, Aperia A, Nielsen S, Nairn A. Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue. American Journal Of Physiology 1999, 276: f254-f259. PMID: 9950956, DOI: 10.1152/ajprenal.1999.276.2.f254.Peer-Reviewed Original ResearchConceptsPhosphorylation of AQP2Protein kinase AAquaporin-2Two-dimensional phosphopeptide mappingCAMP-dependent protein kinase AConsensus phosphorylation sitesActivation of PKAPhosphopeptide mappingPhosphorylation sitesMaximal phosphorylationAQP2 phosphorylationKinase APhosphorylationSer256Immunoblot analysis
1995
Modulation of calcium currents by a D1 dopaminergic protein kinase/phosphatase cascade in rat neostriatal neurons
Surmeier D, Bargas J, Hemmings H, Nairn A, Greengard P. Modulation of calcium currents by a D1 dopaminergic protein kinase/phosphatase cascade in rat neostriatal neurons. Neuron 1995, 14: 385-397. PMID: 7531987, DOI: 10.1016/0896-6273(95)90294-5.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthine2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterAnimalsBrainCalcium Channel BlockersCalcium ChannelsCells, CulturedColforsinCyclic AMPCyclic AMP-Dependent Protein KinasesElectrophysiologyKineticsMembrane PotentialsNeostriatumNeuronsNifedipinePhosphoprotein PhosphatasesProtein Phosphatase 1RatsRats, WistarReceptors, Dopamine D1TetraethylammoniumTetraethylammonium CompoundsTime FactorsConceptsProtein phosphatase 1Protein kinaseInhibition of PP1Cyclic AMP-dependent protein kinaseAMP-dependent protein kinaseInhibition of PKARat neostriatal neuronsPhosphatase cascadePP1 activityReceptor-mediated activationPhosphatase 1Neostriatal neuronsCalcium currentPKA enhancementDifferential regulationHigh voltage-activated calcium currentsVoltage-activated calcium currentsWhole-cell voltage-clamp techniqueD1 pathwayMedium spiny neuronsCyclic AMP analogueD1 dopamine receptorsL-type currentDiversity of effectsSubset of neurons
1994
Role 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
1992
Role of GTP-binding proteins in the regulation of mammalian cardiac chloride conductance.
Hwang T, Horie M, Nairn A, Gadsby D. Role of GTP-binding proteins in the regulation of mammalian cardiac chloride conductance. The Journal Of General Physiology 1992, 99: 465-489. PMID: 1375958, PMCID: PMC2219206, DOI: 10.1085/jgp.99.4.465.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAdenylate Cyclase ToxinAdrenergic beta-AgonistsAnimalsCarbacholCells, CulturedChloride ChannelsChloridesColforsinCyclic AMPGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guinea PigsHeartHistamineIon ChannelsIsoproterenolMembrane ProteinsMyocardiumPertussis ToxinPhosphorylationPropranololReceptors, Adrenergic, betaReceptors, MuscarinicTime FactorsVirulence Factors, BordetellaConceptsProtein kinaseNonhydrolyzable GTP analogG proteinsCAMP-dependent protein kinaseG protein turnoverGTP-binding proteinsCl- conductanceAdenylyl cyclase activityCl- current activationGTP analogueMammalian cardiac myocytesGDP beta SSynthetic peptide inhibitorProtein turnoverStimulatory G proteinMammalian modelsPertussis toxinBeta SInhibitory G proteinBasal activationGTPPeptide inhibitorAdenylyl cyclaseCyclase activityProteinMARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin
Hartwig J, Thelen M, Resen A, Janmey P, Nairn A, Aderem A. MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium–calmodulin. Nature 1992, 356: 618-622. PMID: 1560845, DOI: 10.1038/356618a0.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsBrainCalciumCalmodulinCattleCross-Linking ReagentsHomeostasisIntracellular Signaling Peptides and ProteinsKineticsMembrane ProteinsMicroscopy, ElectronMolecular Sequence DataMusclesMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationProtein Kinase CProteinsRabbitsTime FactorsConceptsProtein kinase CPlasma membraneCalcium-calmodulinKinase CSignal transduction pathwaysPKC signal transduction pathwayActin filament crosslinking proteinActin cytoskeletonActin assemblyTransduction pathwaysMARCKS proteinFilamentous actinCrosslinking activitySpecific substratesSubstrates bindMARCKSCell morphologyProteinPhosphorylationActinMembraneCytoskeletonCalmodulinCytoplasmBinds
1989
Thrombin 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