2014
Nuclear Translocation and Regulation of Intranuclear Distribution of Cytoplasmic Poly(A)-Binding Protein Are Distinct Processes Mediated by Two Epstein Barr Virus Proteins
Park R, El-Guindy A, Heston L, Lin SF, Yu KP, Nagy M, Borah S, Delecluse HJ, Steitz J, Miller G. Nuclear Translocation and Regulation of Intranuclear Distribution of Cytoplasmic Poly(A)-Binding Protein Are Distinct Processes Mediated by Two Epstein Barr Virus Proteins. PLOS ONE 2014, 9: e92593. PMID: 24705134, PMCID: PMC3976295, DOI: 10.1371/journal.pone.0092593.Peer-Reviewed Original ResearchConceptsHost gene expressionIntranuclear distributionZEBRA mutantsReplication proteinsNuclear translocationGene expressionEssential replication proteinViral replication proteinsDownstream viral genesViral replication compartmentsLytic replicationNew protein synthesisBZIP proteinsGlobal shutoffViral alkaline nucleaseReplication compartmentsPABPCEssential functionsEpstein-Barr virus proteinsHost shutoffViral genesLytic programProtein synthesisBinding proteinProtein
2010
miR-29 and miR-30 regulate B-Myb expression during cellular senescence
Martinez I, Cazalla D, Almstead LL, Steitz JA, DiMaio D. miR-29 and miR-30 regulate B-Myb expression during cellular senescence. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 108: 522-527. PMID: 21187425, PMCID: PMC3021067, DOI: 10.1073/pnas.1017346108.Peer-Reviewed Original ResearchConceptsB-myb expressionCellular senescenceMiR-30MiR-29Reporter constructsEndogenous B-MybMajor tumor suppressor mechanismTumor suppressor mechanismIrreversible growth arrestMicroRNA familiesMutant 3'UTRCellular DNA synthesisB-MybReplicative senescenceCompensatory mutationsGrowth arrestMutant sitesRb pathwaySenescenceSuppressor mechanismDNA synthesisRepressionInhibits senescenceExpressionMutations
2001
Communication of the Position of Exon-Exon Junctions to the mRNA Surveillance Machinery by the Protein RNPS1
Lykke-Andersen J, Shu M, Steitz J. Communication of the Position of Exon-Exon Junctions to the mRNA Surveillance Machinery by the Protein RNPS1. Science 2001, 293: 1836-1839. PMID: 11546874, DOI: 10.1126/science.1062786.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsAnimalsCell LineDNA-Binding ProteinsExonsFungal ProteinsGlobinsHeLa CellsHumansMacromolecular SubstancesMiceModels, BiologicalPrecipitin TestsProtein BindingRecombinant Fusion ProteinsRibonucleoproteinsRNA HelicasesRNA SplicingRNA, MessengerRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTransfectionConceptsNonsense-mediated decayExon-exon junctionsMRNA surveillanceMRNA quality controlMRNA surveillance machinerySelective nuclear exportBeta-globin mRNAPremature termination codonUpf complexMature mRNASurveillance machineryNuclear exportAberrant mRNAsMammalian cellsTermination codonUntranslated regionSplice junctionsRNPS1MRNADual roleCentral componentComplexesCodonSubunitsMachinery
2000
Human Upf Proteins Target an mRNA for Nonsense-Mediated Decay When Bound Downstream of a Termination Codon
Lykke-Andersen J, Shu M, Steitz J. Human Upf Proteins Target an mRNA for Nonsense-Mediated Decay When Bound Downstream of a Termination Codon. Cell 2000, 103: 1121-1131. PMID: 11163187, DOI: 10.1016/s0092-8674(00)00214-2.Peer-Reviewed Original ResearchConceptsNonsense-mediated decayExon-exon junctionsTermination codonMRNA exon-exon junctionsNovel human proteinTranslation termination siteHeLa cell extractsBeta-globin mRNAPremature termination codonUpf proteinsEukaryotic cellsAberrant mRNAsHuman proteinsTermination sitesIntact cellsCell extractsCodonHUpf2ProteinMRNAHUpf1CellsCytoplasmCytoplasmicTethering