2017
An Exportin-1–dependent microRNA biogenesis pathway during human cell quiescence
Martinez I, Hayes KE, Barr JA, Harold AD, Xie M, Bukhari SIA, Vasudevan S, Steitz JA, DiMaio D. An Exportin-1–dependent microRNA biogenesis pathway during human cell quiescence. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e4961-e4970. PMID: 28584122, PMCID: PMC5488920, DOI: 10.1073/pnas.1618732114.Peer-Reviewed Original ResearchConceptsBiogenesis pathwayExportin 1Exportin-5Canonical miRNA biogenesis pathwayCanonical miRNA biogenesisTrimethylguanosine synthase 1MicroRNA biogenesis pathwayMiRNA biogenesis pathwayMiRNA processing pathwayStem cell biologyCellular growth arrestGroup of miRNAsExpression of miRNAsPrimary human fibroblastsMiRNA biogenesisPrimary miRNAsCellular quiescenceTissue homeostasisCell biologyProliferative arrestSpecific miRNAsCell quiescenceGrowth arrestBiogenesisMiRNAs
2012
Tracking expression and subcellular localization of RNA and protein species using high-throughput single cell imaging flow cytometry
Borah S, Nichols LA, Hassman LM, Kedes DH, Steitz JA. Tracking expression and subcellular localization of RNA and protein species using high-throughput single cell imaging flow cytometry. RNA 2012, 18: 1573-1579. PMID: 22745225, PMCID: PMC3404377, DOI: 10.1261/rna.033126.112.Peer-Reviewed Original ResearchConceptsKaposi's sarcoma-associated herpesvirusSarcoma-associated herpesvirusSubcellular localizationProtein moleculesHigh-throughput approachPAN RNAProtein speciesNoncoding RNAsNuclear RNAProtein C1Imaging Flow CytometryFlow cytometryRNANuclear translocationHigh-throughput applicationsLytic phaseViral RNATranslocationExpressionLocalizationCellsHeterogeneous populationPABPC1CytometryMolecules
2006
Metazoan oocyte and early embryo development program: a progression through translation regulatory cascades
Vasudevan S, Seli E, Steitz JA. Metazoan oocyte and early embryo development program: a progression through translation regulatory cascades. Genes & Development 2006, 20: 138-146. PMID: 16418480, DOI: 10.1101/gad.1398906.Peer-Reviewed Original ResearchAnimalsCarrier ProteinsCell Cycle ProteinsCytoplasmFemaleGene Expression Regulation, DevelopmentalHumansMaleModels, GeneticMRNA Cleavage and Polyadenylation FactorsOocytesPoly(A)-Binding ProteinsPolyadenylationProtein BiosynthesisRNA-Binding ProteinsRNA, Messenger, StoredTranscription FactorsXenopus laevisXenopus Proteins
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-Binding ProteinsRNA, MessengerConceptsAU-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 ResearchHuR 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-Binding ProteinsRNA, MessengerSequence 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
A new method for detecting sites of 2'-O-methylation in RNA molecules.
Yu YT, Shu MD, Steitz JA. A new method for detecting sites of 2'-O-methylation in RNA molecules. RNA 1997, 3: 324-31. PMID: 9056769, PMCID: PMC1369484.Peer-Reviewed Original ResearchConceptsRNA moleculesEukaryotic ribosomal RNALong RNA moleculesSpecific rRNARibosomal RNAModification sitesRRNAMethylationCell nucleoliChimeric oligonucleotideSnoRNAsRNase H cleavagePrecursor moleculesRRNA transportSitesMoleculesRNANucleotidesCytoplasmNucleoliResiduesCleavageOligonucleotideH cleavageNucleus
1991
Structural analyses of the 7SK ribonucleoprotein (RNP), the most abundant human small RNP of unknown function.
Wassarman DA, Steitz JA. Structural analyses of the 7SK ribonucleoprotein (RNP), the most abundant human small RNP of unknown function. Molecular And Cellular Biology 1991, 11: 3432-3445. PMID: 1646389, PMCID: PMC361072, DOI: 10.1128/mcb.11.7.3432.Peer-Reviewed Original Research
1981
Snurps and scyrps
Lerner M, Steitz J. Snurps and scyrps. Cell 1981, 25: 298-300. PMID: 6169438, DOI: 10.1016/0092-8674(81)90047-7.Peer-Reviewed Original Research