2005
A molecular switch for translational control in taste memory consolidation
Belelovsky K, Elkobi A, Kaphzan H, Nairn A, Rosenblum K. A molecular switch for translational control in taste memory consolidation. European Journal Of Neuroscience 2005, 22: 2560-2568. PMID: 16307598, DOI: 10.1111/j.1460-9568.2005.04428.x.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2Protein synthesisEEF2 phosphorylationKinase 2 activationElongation factor 2Translational regulationTranslation initiationTranslational controlS6K1 phosphorylationMolecular switchSwitch-like effectNeuronal proteinsPhosphorylationElongation rateRate-limiting stepFactor 2Taste memory consolidationSynaptoneurosomal fractionsExpressionTemporal patternsInitiation rateProtein
2001
Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †
Chen Y, Matsushita M, Nairn A, Damuni Z, Cai D, Frerichs K, Hallenbeck J. Mechanisms for Increased Levels of Phosphorylation of Elongation Factor-2 during Hibernation in Ground Squirrels †. Biochemistry 2001, 40: 11565-11570. PMID: 11560506, DOI: 10.1021/bi010649w.Peer-Reviewed Original ResearchConceptsEukaryotic elongation factor 2EEF-2 phosphorylationElongation factor 2Elongation phaseEEF-2 kinase activityProtein phosphatase 2AGround squirrelsLevel of phosphorylationFactor 2Phosphatase 2ACellular functionsCatalytic subunitUncharacterized mechanismKinase activityInhibitor 2Protein synthesisPhosphorylationPP2AHibernating animalsActive animalsHibernatorsReversible mechanismSevere reductionSquirrelsHibernation
1997
Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA
Cheng X, Höög J, Nairn A, Greengard P, Aperia A. Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA. American Journal Of Physiology 1997, 273: c1981-c1986. PMID: 9435504, DOI: 10.1152/ajpcell.1997.273.6.c1981.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionAnimalsColforsinCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesCytosolDichlororibofuranosylbenzimidazoleEnzyme ActivationHomeostasisIsoenzymesKineticsMutagenesis, Site-DirectedPhorbol 12,13-DibutyratePhosphorylationProtein Kinase CRatsRecombinant ProteinsSerineSodium-Potassium-Exchanging ATPaseThionucleotidesTransfectionConceptsProtein kinase AProtein kinase CATPase alpha 1State of phosphorylationEffect of PKCWild-type enzymeSpecific PKA activatorActivity of PKCEnzyme activityAlpha 1Direct phosphorylationCOS cellsATPase alphaKinase ASer-23Kinase CPKA activatorPhosphorylationPKA systemPhorbol esterATPase activityMutantsEffect of PDBuCellsInhibition
1987
Nerve growth factor treatment or cAMP elevation reduces Ca2+/calmodulin-dependent protein kinase III activity in PC12 cells.
Nairn A, Nichols R, Brady M, Palfrey H. Nerve growth factor treatment or cAMP elevation reduces Ca2+/calmodulin-dependent protein kinase III activity in PC12 cells. Journal Of Biological Chemistry 1987, 262: 14265-14272. PMID: 2443502, DOI: 10.1016/s0021-9258(18)47933-1.Peer-Reviewed Original ResearchConceptsNerve growth factorEffect of forskolinIII activityPC12 cellsGrowth factorLong-term treatmentShort-term treatmentEffect of treatmentNerve growth factor treatmentGrowth factor treatmentAbility of forskolinAbility of NGFPhorbol esterEpidermal growth factorMaximal effectCytosolic extractsFactor treatmentForskolinCAMP elevationTreatmentCell linesProtein kinase CRemoval of forskolinImmunological techniquesDependent protein phosphorylation
1985
Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues.
Nairn A, Bhagat B, Palfrey H. Identification of calmodulin-dependent protein kinase III and its major Mr 100,000 substrate in mammalian tissues. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 7939-7943. PMID: 3906654, PMCID: PMC390885, DOI: 10.1073/pnas.82.23.7939.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseCaM kinase IIIKinase IIIProtein kinaseMammalian tissuesCalmodulin-dependent protein kinase IIIProtein kinase IIIDependent protein kinaseProtein phosphorylation systemsWidespread tissue distributionTotal cytosolic proteinAnimal cellsPhosphorylation systemSubstrate specificityCytosolic proteinsMyosin light chainMajor substrateKinaseProteinSynapsin IPoor substrateCell linesPhosphorylase bMajor MrPolyclonal antibodies