2004
Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses
Mili S, Steitz JA. Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses. RNA 2004, 10: 1692-1694. PMID: 15388877, PMCID: PMC1370654, DOI: 10.1261/rna.7151404.Peer-Reviewed Original ResearchThe Herpesvirus saimiri Small Nuclear RNAs Recruit AU-Rich Element-Binding Proteins but Do Not Alter Host AU-Rich Element-Containing mRNA Levels in Virally Transformed T Cells
Cook HL, Mischo HE, Steitz JA. The Herpesvirus saimiri Small Nuclear RNAs Recruit AU-Rich Element-Binding Proteins but Do Not Alter Host AU-Rich Element-Containing mRNA Levels in Virally Transformed T Cells. Molecular And Cellular Biology 2004, 24: 4522-4533. PMID: 15121869, PMCID: PMC400482, DOI: 10.1128/mcb.24.10.4522-4533.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, SurfaceBase CompositionBase SequenceCallithrixCell LineCell Transformation, ViralELAV ProteinsELAV-Like Protein 1Herpesvirus 2, SaimiriineHeterogeneous-Nuclear Ribonucleoprotein DIn Vitro TechniquesMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingRNA-Binding ProteinsRNA, MessengerRNA, Small NuclearRNA, ViralT-LymphocytesConceptsAU-rich elementsSmall nuclear RNAHSURs 1Herpesvirus saimiriNuclear RNAMRNA decay pathwayMarmoset T cellsHSUR 1HnRNP DPosttranscriptional regulationHost mRNAsHost proteinsMicroarray analysisUnknown functionProtein tristetraprolinVivo interactionDecay pathwaysHSURsMRNARNAMRNA levelsT cellsProteinCellsPathwayTransportins 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
Delineation of mRNA Export Pathways by the Use of Cell-Permeable Peptides
Gallouzi I, Steitz J. Delineation of mRNA Export Pathways by the Use of Cell-Permeable Peptides. Science 2001, 294: 1895-1901. PMID: 11729309, DOI: 10.1126/science.1064693.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntennapedia Homeodomain ProteinAntigens, SurfaceBiological TransportCell LineCell Membrane PermeabilityCell NucleusCytoplasmELAV ProteinsELAV-Like Protein 1Genes, fosHeat-Shock ResponseHomeodomain ProteinsHumansKaryopherinsMolecular Sequence DataNeuropeptidesNuclear ProteinsPeptide FragmentsPhosphoproteinsProtein BindingProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearRegulatory Sequences, Nucleic AcidReproducibility of ResultsRNA StabilityRNA-Binding ProteinsRNA, MessengerTetrahydrofolate DehydrogenaseTranscription FactorsConceptsNuclear export signalAU-rich elementsMessenger RNAsAdapter proteinCell-permeable peptideLeucine-rich nuclear export signalReceptor proteinMRNA export pathwayNuclear pore complexExport receptor CRM1Overall cellular distributionSitu hybridization experimentsMRNA exportExport signalNucleocytoplasmic shuttlingPore complexExport pathwayHybridization experimentsProtein ligandsCellular distributionProteinProtein 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 genesHuR and mRNA stability
Brennan CM, Steitz* J. HuR and mRNA stability. Cellular And Molecular Life Sciences 2001, 58: 266-277. PMID: 11289308, PMCID: PMC11146503, DOI: 10.1007/pl00000854.Peer-Reviewed Original ResearchConceptsAU-rich elementsMessenger RNAsGene regulationMRNA decayPosttranscriptional gene regulationMRNA degradation pathwayDrosophila ELAVMammalian cellsHu familyHuR functionMRNA stabilityUntranslated regionStressed cellsProtein ligandsRole of HuRCultured cellsEnvironmental changesHuRDegradation pathwayRapid degradationImportant mechanismRegulationCellsELAVRNAs
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 regionHuR binding to cytoplasmic mRNA is perturbed by heat shock
Gallouzi I, Brennan C, Stenberg M, Swanson M, Eversole A, Maizels N, Steitz J. HuR binding to cytoplasmic mRNA is perturbed by heat shock. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 3073-3078. PMID: 10737787, PMCID: PMC16194, DOI: 10.1073/pnas.97.7.3073.Peer-Reviewed Original Research
1998
HNS, a nuclear-cytoplasmic shuttling sequence in HuR
Fan X, Steitz J. HNS, a nuclear-cytoplasmic shuttling sequence in HuR. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 15293-15298. PMID: 9860962, PMCID: PMC28036, DOI: 10.1073/pnas.95.26.15293.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAntigens, SurfaceCell NucleusConserved SequenceCytoplasmELAV ProteinsELAV-Like Protein 1HeLa CellsHeterogeneous-Nuclear Ribonucleoprotein KHumansMiceMolecular Sequence DataRecombinant ProteinsRibonucleoproteinsRNA, MessengerRNA-Binding ProteinsSequence AlignmentSequence Homology, Amino AcidTransfectionXenopusConceptsHeterogeneous nuclear ribonucleoprotein KNuclear localization signal activityClassical nuclear localization signalAU-rich element-containing mRNAsExport of mRNAHeterogeneous nuclear ribonucleoprotein A1Nuclear export signalNuclear localization signalNuclear transport processRNA-binding proteinAU-rich elementsExport signalLocalization signalM9 sequenceNuclear poresDomain sequencesCytoplasmic compartmentUntranslated regionLabile mRNAsCell nucleiSpecific signalsHuRProteinBidirectional transportMRNAOverexpression of HuR, a nuclear–cytoplasmic shuttling protein, increases the in vivo stability of ARE‐containing mRNAs
Fan X, Steitz J. Overexpression of HuR, a nuclear–cytoplasmic shuttling protein, increases the in vivo stability of ARE‐containing mRNAs. The EMBO Journal 1998, 17: 3448-3460. PMID: 9628880, PMCID: PMC1170681, DOI: 10.1093/emboj/17.12.3448.Peer-Reviewed Original ResearchConceptsAU-rich elementsOverexpression of HuRUntranslated regionRNA recognition motif 3Beta-globin reporter mRNAClass II AU-rich elementsAnti-HuR antibodyMouse L929 cellsMRNA decayELAV familyVivo decay ratesDeletion mutantsReporter mRNAL929 cellsMotif 3HuR functionMRNA stabilityCytoplasmic compartmentRNA sequencesRRMs 3HuR proteinVivo roleMessenger RNAHuRHuR antibody
1997
AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation
Fan X, Myer V, Steitz J. AU-rich elements target small nuclear RNAs as well as mRNAs for rapid degradation. Genes & Development 1997, 11: 2557-2568. PMID: 9334320, PMCID: PMC316563, DOI: 10.1101/gad.11.19.2557.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, SurfaceBase SequenceELAV ProteinsELAV-Like Protein 1Gene Expression RegulationGenes, ReporterGlobinsHerpesvirus 2, SaimiriineMolecular Sequence DataMutationRepetitive Sequences, Nucleic AcidRibonucleasesRNA, MessengerRNA, Small NuclearRNA, ViralRNA-Binding ProteinsTranscription, GeneticTransfectionConceptsAU-rich elementsMRNA degradation machinerySmall nuclear RNAHSUR 1Host RNA moleculesDegradation machineryMammalian mRNAsNuclear RNARNA moleculesMutational analysisSequence requirementsTarget RNAHuR proteinOngoing translationRNA 1MRNARapid degradationRNASimilar mechanismDegradation activityDeadenylationSnRNAMachineryProteinDegradationIdentification of HuR as a protein implicated in AUUUA‐mediated mRNA decay
Myer V, Fan X, Steitz J. Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay. The EMBO Journal 1997, 16: 2130-2139. PMID: 9155038, PMCID: PMC1169815, DOI: 10.1093/emboj/16.8.2130.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAntigens, SurfaceBase CompositionCell ExtractsCross-Linking ReagentsELAV ProteinsELAV-Like Protein 1Gene Expression RegulationHeLa CellsHumansMiceMolecular Sequence DataMolecular WeightRegulatory Sequences, Nucleic AcidRNA-Binding ProteinsRNA, MessengerUltraviolet RaysConceptsAU-rich elementsMRNA decayUntranslated regionRNA-binding specificityARE-binding proteinsHeLa nuclear extractsGene familyMRNA degradationNuclear extractsEssential signalMessenger RNAProteinSequence's abilityHuRAUUUARapid degradationCritical roleHuR.RNAMachineryMRNADegradationRegulationSubsequent analysisExpression
1986
Characterization of the DNA-binding protein antigen Ku recognized by autoantibodies from patients with rheumatic disorders.
Mimori T, Hardin JA, Steitz JA. Characterization of the DNA-binding protein antigen Ku recognized by autoantibodies from patients with rheumatic disorders. Journal Of Biological Chemistry 1986, 261: 2274-2278. PMID: 3511059, DOI: 10.1016/s0021-9258(17)35929-x.Peer-Reviewed Original ResearchConceptsKu proteinNovel DNA-binding proteinAnti-Ku antibodiesDNA-binding proteinsHigh molecular weight nucleic acidsExtracts of cellsKu antigenDa subunitChromatinHeLa cellsScleroderma-polymyositis overlap syndromeBiochemical natureProteinWeight nucleic acidsLarge formNucleic acidsOverlap syndromeRheumatic disordersCertain patientsAntibodiesAntigenAutoantibodiesCellsImmunoaffinity column chromatographyPatients