2001
Elongation 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
1995
Rapamycin inhibits ribosomal protein synthesis and induces G1 prolongation in mitogen-activated T lymphocytes.
Terada N, Takase K, Papst P, Nairn A, Gelfand E. Rapamycin inhibits ribosomal protein synthesis and induces G1 prolongation in mitogen-activated T lymphocytes. The Journal Of Immunology 1995, 155: 3418-26. PMID: 7561036, DOI: 10.4049/jimmunol.155.7.3418.Peer-Reviewed Original ResearchConceptsCell cycle progressionRibosomal protein mRNAsCycle progressionG2/M phaseRibosomal proteinsProtein synthesisProtein mRNAG1 prolongationCell cycleS phaseRibosomal protein mRNA translationRibosomal protein synthesisM phaseTotal cellular proteinEffect of rapamycinDNA synthesisNumber of ribosomesCell sizeCellular proteinsMRNA translation
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 proteins
1993
Phosphorylation 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