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
2006
Epstein-Barr virus noncoding RNAs are confined to the nucleus, whereas their partner, the human La protein, undergoes nucleocytoplasmic shuttling
Fok V, Friend K, Steitz JA. Epstein-Barr virus noncoding RNAs are confined to the nucleus, whereas their partner, the human La protein, undergoes nucleocytoplasmic shuttling. Journal Of Cell Biology 2006, 173: 319-325. PMID: 16682524, PMCID: PMC2063832, DOI: 10.1083/jcb.200601026.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAnimalsAntibiotics, AntineoplasticAutoantigensCell LineCell Line, TumorCell NucleusDactinomycinFatty Acids, UnsaturatedFemaleHeLa CellsHerpesvirus 4, HumanHumansKaryopherinsMiceNIH 3T3 CellsOocytesProtein BindingRibonucleoproteinsRNA TransportRNA, UntranslatedRNA, ViralXenopus laevis
2004
Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR
Rebane A, Aab A, Steitz JA. Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR. RNA 2004, 10: 590-599. PMID: 15037768, PMCID: PMC1370549, DOI: 10.1261/rna.5224304.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, SurfaceBeta KaryopherinsCell NucleusELAV ProteinsELAV-Like Protein 1HeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHumansMolecular Sequence DataMutationProtein Structure, TertiaryRan GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsSequence Analysis, ProteinConceptsHnRNP A1Transportin-1Import factorsDigitonin-permeabilized HeLa cellsNuclear import factorsMRNA-binding proteinRecombinant hnRNP A1Binding of HuRImp betaImport pathwayCargo specificityNuclear importExport receptorTransportin-2TransportinTransport signalHeLa cellsLikely actsHuRTrn1ProteinInteraction studiesImportTRN2RanGTP
2001
Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock.
Gallouzi IE, Brennan CM, Steitz JA. Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock. RNA 2001, 7: 1348-61. PMID: 11565755, PMCID: PMC1370177, DOI: 10.1017/s1355838201016089.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAntigens, SurfaceCarrier ProteinsCytoplasmELAV ProteinsELAV-Like Protein 1Fatty Acids, UnsaturatedHeat-Shock ResponseHeLa CellsHumansKaryopherinsLigandsNeuropeptidesNuclear ProteinsPhosphoproteinsReceptors, Cytoplasmic and NuclearRNA, MessengerRNA-Binding ProteinsConceptsAU-rich elementsNuclear exportHeat shockMessenger RNANuclear export factor CRM1Protein ligandsInhibitor of CRM1Export factor CRM1CRM1-dependent exportMRNA nuclear exportRNA-binding proteinProtein-protein interactionsRapid mRNA turnoverEarly response genesAssociation of HuRHeat shock inducesCytoplasmic fociHnRNP complexesExport pathwayMRNA turnoverLeptomycin BCoimmunoprecipitation experimentsCytoplasmic interactionsNES domainResponse genesSplicing Factors SRp20 and 9G8 Promote the Nucleocytoplasmic Export of mRNA
Huang Y, Steitz J. Splicing Factors SRp20 and 9G8 Promote the Nucleocytoplasmic Export of mRNA. Molecular Cell 2001, 7: 899-905. PMID: 11336712, DOI: 10.1016/s1097-2765(01)00233-7.Peer-Reviewed Original ResearchInternal Modification of U2 Small Nuclear (Snrna) Occurs in Nucleoli of Xenopus Oocytes
Yu Y, Shu M, Narayanan A, Terns R, Terns M, Steitz J. Internal Modification of U2 Small Nuclear (Snrna) Occurs in Nucleoli of Xenopus Oocytes. Journal Of Cell Biology 2001, 152: 1279-1288. PMID: 11257127, PMCID: PMC2199211, DOI: 10.1083/jcb.152.6.1279.Peer-Reviewed Original ResearchConceptsNucleolar localizationCajal bodiesU2 RNAInternal modificationSmall nuclearSm binding siteNucleolar localization signalSmall nucleolar RNAsXenopus oocytesCytoplasm of oocytesU2 small nuclearGuanosine capLocalization signalNucleolar RNAsRNAs showSubcellular sitesIntranuclear localizationIsolated nucleiRNABinding sitesNucleoliOocytesNucleotidesCytoplasmU2
2000
Protein Ligands to Hur Modulate Its Interaction with Target Mrnas in Vivo
Brennan C, Gallouzi I, Steitz J. Protein Ligands to Hur Modulate Its Interaction with Target Mrnas in Vivo. Journal Of Cell Biology 2000, 151: 1-14. PMID: 11018049, PMCID: PMC2189805, DOI: 10.1083/jcb.151.1.1.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, SurfaceBinding SitesCarrier ProteinsChromatography, AffinityCytoplasmELAV ProteinsELAV-Like Protein 1Fatty Acids, UnsaturatedHeLa CellsHumansKaryopherinsLigandsMolecular Sequence DataNeuropeptidesNuclear ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein BindingProtein Phosphatase 2Protein TransportReceptors, Cytoplasmic and NuclearRNA StabilityRNA-Binding ProteinsRNA, MessengerSequence Analysis, ProteinConceptsAU-rich elementsTarget mRNAsStability of ARENuclear export factor CRM1Protein phosphatase 2A inhibitorExport factor CRM1Phosphatase 2A inhibitorCOOH-terminal tailInhibition of CRM1Leucine-rich repeatsC-fos geneMammalian proteinsLeptomycin BELAV familyCellular mRNAsNuclear retentionSecond motifHuR associationUntranslated regionBind regionsCytoplasmic distributionPp32Protein ligandsCRM1Terminal region