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 reductionSquirrelsHibernationElongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium
Nairn A, Matsushita M, Nastiuk K, Horiuchi A, Mitsui K, Shimizu Y, Palfrey H. Elongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium. Progress In Molecular And Subcellular Biology 2001, 27: 91-129. PMID: 11575162, DOI: 10.1007/978-3-662-09889-9_4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCell CycleCell DivisionCyclic AMP-Dependent Protein KinasesCysteine EndopeptidasesElongation Factor 2 KinaseHumansMolecular Sequence DataMultienzyme ComplexesNeuronsPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2PhosphorylationProteasome Endopeptidase ComplexProtein BiosynthesisSequence Homology, Amino AcidSignal TransductionUbiquitinConceptsProtein synthesisElongation factor 2 phosphorylationDephosphorylation of eEF2Eukaryotic protein synthesisAminoacyl-tRNA synthetasesFactor 2 phosphorylationElongation factor 2Ribosomal proteinsRegulated processInitiation factorsDependent kinasesKey proteinsRate of elongationPeptidyl-tRNAPhysiological roleKinasePhosphorylationFactor 2EEF2P siteThr56ProteinSynthetasesDephosphorylationRibosomes
2000
Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase
Cho S, Koketsu M, Ishihara H, Matsushita M, Nairn A, Fukazawa H, Uehara Y. Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase. Biochimica Et Biophysica Acta 2000, 1475: 207-215. PMID: 10913818, DOI: 10.1016/s0304-4165(00)00061-1.Peer-Reviewed Original ResearchConceptsV-src-transformed NIH3T3 cellsEukaryotic elongation factor 2 kinaseProtein kinase AElongation factor 2 kinaseProtein kinase CProtein tyrosine kinasesEEF-2KProtein kinaseEEF-2K inhibitorNIH3T3 cellsCalmodulin-dependent protein kinaseV-Src kinaseMultiple protein kinasesCalmodulin-dependent protein kinase IIProtein levelsK inhibitorsProtein kinase IIEEF-2K.Kinase AKinase IITyrosine kinaseKinase CKinaseTs-4Specific inhibitor
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
1990
Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase
Brady M, Nairn A, Wagner J, Palfrey H. Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase. Journal Of Neurochemistry 1990, 54: 1034-1039. PMID: 1689374, DOI: 10.1111/j.1471-4159.1990.tb02354.x.Peer-Reviewed Original ResearchConceptsWild-type cellsCalmodulin-dependent protein kinase IIICAMP-dependent protein kinase activityProtein kinase IIIProtein kinase activityEpidermal growth factorKinase IIIKinase activityA126-1B2 cellsCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePC12 cellsNerve growth factorMutant PC12 cell lineElongation factor 2Growth factorAbility of NGFPC12 cell lineEffects of NGFProtein kinaseNGF additionA126-1B2Down regulationCell linesFactor 2Role 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
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 phosphorylationRapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients.
Palfrey H, Nairn A, Muldoon L, Villereal M. Rapid activation of calmodulin-dependent protein kinase III in mitogen-stimulated human fibroblasts. Correlation with intracellular Ca2+ transients. Journal Of Biological Chemistry 1987, 262: 9785-9792. PMID: 3496338, DOI: 10.1016/s0021-9258(18)48002-7.Peer-Reviewed Original Research