2024
PTH-dependent stabilization of RANKL mRNA is associated with increased phosphorylation of the KH-type splicing regulatory protein
Yao G, Zhu M, Insogna K. PTH-dependent stabilization of RANKL mRNA is associated with increased phosphorylation of the KH-type splicing regulatory protein. Molecular And Cellular Endocrinology 2024, 595: 112412. PMID: 39536935, DOI: 10.1016/j.mce.2024.112412.Peer-Reviewed Original ResearchReceptor activator of nuclear factor kappa-B ligandReceptor activator of nuclear factor kappa-B ligand mRNAAU-rich elementsParathyroid hormone treatmentParathyroid hormoneMRNA stabilityRegulation of mRNA stabilityAU-rich element-binding proteinBinding to AU-rich elementsActivation of transcriptionInhibition of cellular transcriptionRegulate mRNA stabilityCells treated with vehicleSplicing regulatory proteinKH-type splicing regulatory proteinNuclear factor kappa-B ligandAU-RichElement-binding proteinTNF family membersCellular transcriptionAssociated with increased phosphorylationPTH exposureRegulatory proteinsBinding proteinCells pre-treatedMultiple roles for AU-rich RNA binding proteins in the development of haematologic malignancies and their resistance to chemotherapy
Podszywalow-Bartnicka P, Neugebauer K. Multiple roles for AU-rich RNA binding proteins in the development of haematologic malignancies and their resistance to chemotherapy. RNA Biology 2024, 21: 584-600. PMID: 38798162, PMCID: PMC11135835, DOI: 10.1080/15476286.2024.2346688.Peer-Reviewed Original ResearchConceptsARE-binding proteinsRNA-binding proteinsAU-rich elementsStress granulesBinding proteinTranslational regulation of mRNAsImpact alternative splicingCytoplasmic stress granulesProtein-RNA bindingAdaptation to microenvironmentProtein-RNA networksBinding to AU-rich elementsCancer cell proteomePost-transcriptional regulationAU-rich RNA-binding proteinsRegulation of mRNAsChemotherapy resistanceGene expression levelsSequence motifsProtein-RNAMRNA structureMature mRNATranslational regulationAlternative splicingCell proteomeUPF1 regulates mRNA stability by sensing poorly translated coding sequences
Musaev D, Abdelmessih M, Vejnar C, Yartseva V, Weiss L, Strayer E, Takacs C, Giraldez A. UPF1 regulates mRNA stability by sensing poorly translated coding sequences. Cell Reports 2024, 43: 114074. PMID: 38625794, PMCID: PMC11259039, DOI: 10.1016/j.celrep.2024.114074.Peer-Reviewed Original ResearchConceptsUpstream open reading framesOpen reading frameRegulate mRNA stabilityNonsense-mediated decayMRNA stabilityReading frameOpen reading frame lengthRegulate mRNA decayAU-rich elementsMicroRNA Binding SitesCis-elementsTranslation initiationStop codonMRNA decayCodon optimizationUPF1Gene expressionBinding sitesCodonMRNAConvergent rolesHigher decay ratesMachine-learning analysisUTR
2019
Genome wide analysis of 3′ UTR sequence elements and proteins regulating mRNA stability during maternal-to-zygotic transition in zebrafish
Vejnar CE, Messih M, Takacs C, Yartseva V, Oikonomou P, Christiano R, Stoeckius M, Lau S, Lee M, Beaudoin JD, Musaev D, Darwich-Codore H, Walther T, Tavazoie S, Cifuentes D, Giraldez A. Genome wide analysis of 3′ UTR sequence elements and proteins regulating mRNA stability during maternal-to-zygotic transition in zebrafish. Genome Research 2019, 29: 1100-1114. PMID: 31227602, PMCID: PMC6633259, DOI: 10.1101/gr.245159.118.Peer-Reviewed Original ResearchConceptsAU-rich elementsMRNA stabilityZygotic transitionRich motifGenome-wide analysisRNA-protein interactionsGenome activationParallel reporterCombinatorial regulationMaternal transcriptsMiR-430Destabilizing motifsRegulatory motifsWide analysisMRNA deadenylationPosttranscriptional regulationRegulatory sequencesMost transcriptsMultiple decay pathwaysUTR sequencesSequence elementsGene expressionTarget sequenceDecay pathwaysMotif
2018
T cell LFA-1-induced proinflammatory mRNA stabilization is mediated by the p38 pathway kinase MK2 in a process regulated by hnRNPs C, H1 and K
Rao GK, Wong A, Collinge M, Sarhan J, Yarovinsky TO, Ramgolam VS, Gaestel M, Pardi R, Bender JR. T cell LFA-1-induced proinflammatory mRNA stabilization is mediated by the p38 pathway kinase MK2 in a process regulated by hnRNPs C, H1 and K. PLOS ONE 2018, 13: e0201103. PMID: 30048492, PMCID: PMC6065199, DOI: 10.1371/journal.pone.0201103.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Culture TechniquesCytoplasmELAV-Like Protein 1Heterogeneous-Nuclear RibonucleoproteinsHumansIntracellular Signaling Peptides and ProteinsJurkat CellsLymphocyte Function-Associated Antigen-1Mice, Inbred C57BLMice, KnockoutProtein Serine-Threonine KinasesProteomeRNA StabilityRNA, MessengerSignal TransductionT-LymphocytesConceptsKinase MK2Β2-integrin lymphocyte function-associated antigen-1AU-rich elementsLymphocyte function-associated antigen-1Integrin lymphocyte function-associated antigen-1HuR localizationProtein HuR.Key regulatorMRNA stabilizationCritical activatorCytoplasmic translocationHuR activitySequential activationHuRIntricate processFunction-associated antigen-1MRNAEngagement resultsMK2Antigen 1H1ActivationHnRNPsHuR.Transcripts
2012
AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus
Lee N, Pimienta G, Steitz JA. AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus. RNA 2012, 18: 2073-2082. PMID: 23012480, PMCID: PMC3479396, DOI: 10.1261/rna.034900.112.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsAptamers, NucleotideAU Rich ElementsBinding, CompetitiveCell Line, TumorHerpesvirus 4, HumanHeterogeneous Nuclear Ribonucleoprotein D0Heterogeneous-Nuclear Ribonucleoprotein DHost-Pathogen InteractionsHumansImmunoprecipitationMutagenesis, InsertionalProtein BindingProtein IsoformsRNA StabilityRNA, ViralConceptsAU-rich elementsProtein partnersAUF1/hnRNP DUntranslated regionBacteriophage MS2 coat proteinNovel protein partnersHigh abundanceElectrophoretic mobility shift assaysEpstein-Barr virusMS2 coat proteinStable isotope labelingMobility shift assaysInteracting proteinMolecular functionsHnRNP DAlternative splicingNoncoding RNAsShift assaysCoat proteinIsotope labelingP40 isoformRNA aptamersRNA 1AUF1UV crosslinkingThe mRNA‐Binding Protein Zfp36 Is Upregulated by β‐Adrenergic Stimulation and Represses IL‐6 Production in 3T3‐L1 Adipocytes
Brahma PK, Zhang H, Murray BS, Shu F, Sidell N, Seli E, Kallen CB. The mRNA‐Binding Protein Zfp36 Is Upregulated by β‐Adrenergic Stimulation and Represses IL‐6 Production in 3T3‐L1 Adipocytes. Obesity 2012, 20: 40-47. PMID: 21818148, PMCID: PMC4127993, DOI: 10.1038/oby.2011.259.Peer-Reviewed Original ResearchConceptsAU-rich elementsZFP36 expressionCell type-specific modulatorsPost-transcriptional levelMRNA-binding proteinRetinoic acidZinc finger protein 36Novel mechanistic approachTarget mRNAsMRNA targetsSuch proteinsPotent repressorAdipocyte-derived IL-6Protein 36Chronic inflammatory stateSystemic immune responsesDevelopment of diabetesDependent pathwayDiverse inflammatory disordersZFP36IL-6 productionAdrenergic receptor agonist isoproterenolCyclic adenosine monophosphateInterleukin-6 expressionΒ-Adrenergic Stimulation
2010
T Cell LFA-1 Engagement Induces HuR-Dependent Cytokine mRNA Stabilization through a Vav-1, Rac1/2, p38MAPK and MKK3 Signaling Cascade
Ramgolam VS, DeGregorio SD, Rao GK, Collinge M, Subaran SS, Markovic-Plese S, Pardi R, Bender JR. T Cell LFA-1 Engagement Induces HuR-Dependent Cytokine mRNA Stabilization through a Vav-1, Rac1/2, p38MAPK and MKK3 Signaling Cascade. PLOS ONE 2010, 5: e14450. PMID: 21206905, PMCID: PMC3012057, DOI: 10.1371/journal.pone.0014450.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, SurfaceCytokinesELAV ProteinsELAV-Like Protein 1GTP PhosphohydrolasesHumansIntegrinsInterferon-gammaLymphocyte Function-Associated Antigen-1MAP Kinase Kinase 3MiceMice, Inbred C57BLNeuropeptidesp38 Mitogen-Activated Protein KinasesProto-Oncogene Proteins c-vavrac GTP-Binding Proteinsrac1 GTP-Binding ProteinRNA-Binding ProteinsSignal TransductionT-LymphocytesTumor Necrosis Factor-alphaDown-Regulation of a Host microRNA by a Viral Noncoding RNA
Cazalla D, Steitz JA. Down-Regulation of a Host microRNA by a Viral Noncoding RNA. Cold Spring Harbor Symposia On Quantitative Biology 2010, 75: 321-324. PMID: 21139068, PMCID: PMC5647998, DOI: 10.1101/sqb.2010.75.009.Peer-Reviewed Original ResearchConceptsHerpesvirus saimiriNoncoding RNAsHost cell gene expressionMiR-27Binding-dependent mannerAU-rich elementsViral noncoding RNAMarmoset T cellsMiRNA pathwayHost cell microRNAsViral life cycleConserved sequencesEctopic expressionMammalian virusesTarget genesTransient knockdownMutational analysisGene expressionHost microRNAsHSUR1Viral strategiesBase pairingDown regulationPrimate herpesvirusesLytic phase
2008
Cell cycle control of microRNA-mediated translation regulation
Vasudevan S, Tong Y, Steitz JA. Cell cycle control of microRNA-mediated translation regulation. Cell Cycle 2008, 7: 1545-1549. PMID: 18469529, PMCID: PMC2556257, DOI: 10.4161/cc.7.11.6018.Peer-Reviewed Original Research
2007
Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation
Vasudevan S, Tong Y, Steitz JA. Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation. Science 2007, 318: 1931-1934. PMID: 18048652, DOI: 10.1126/science.1149460.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsArgonaute ProteinsBase PairingCell CycleCell LineCell ProliferationComputational BiologyEukaryotic Initiation Factor-2Gene Expression RegulationHeLa CellsHMGA2 ProteinHumansInterphaseMicroRNAsProtein BiosynthesisRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerTransfectionTumor Necrosis Factor-alphaUp-RegulationConceptsAU-rich elementsCell cycle arrestCycle arrestUntranslated regionMental retardation-related protein 1MicroRNA target sitesMicroRNA let-7Messenger RNA (mRNA) 3' untranslated regionsRegulates TranslationTranslation regulationTarget mRNAsGene expressionCell cycleCommon functionProtein 1ArgonauteTarget siteActivation signalsRepressionTumor necrosis factor-alpha mRNAMRNARegulationActivationArrestMicroRNPsAU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2
Vasudevan S, Steitz JA. AU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2. Cell 2007, 128: 1105-1118. PMID: 17382880, PMCID: PMC3430382, DOI: 10.1016/j.cell.2007.01.038.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsArgonaute ProteinsCell CycleCell LineChromatography, AffinityCulture Media, Serum-FreeEukaryotic Initiation Factor-2Genes, ReporterHumansLuciferases, FireflyMonocytesPeptide Initiation FactorsPolyribosomesProtein BiosynthesisRegulatory Sequences, Ribonucleic AcidRibonucleoproteinsRNA-Binding ProteinsSerumTumor Necrosis Factor-alphaUp-RegulationConceptsAU-rich elementsArgonaute 2Posttranscriptional regulatory systemsAffinity purification methodShRNA knockdown experimentsCell cycle arrestHuman cell linesTranslation activationRegulatory signalsMRNA stabilityGene expressionSerum starvationAU-RichFXR1Activation roleRegulatory systemProtein 1Cell linesMRNA levelsNew insightsDevelopmental consequencesTranslation conditionsUpregulationDirect evidencePurification method
2006
LFA-1-Dependent HuR Nuclear Export and Cytokine mRNA Stabilization in T Cell Activation
Wang JG, Collinge M, Ramgolam V, Ayalon O, Fan XC, Pardi R, Bender JR. LFA-1-Dependent HuR Nuclear Export and Cytokine mRNA Stabilization in T Cell Activation. The Journal Of Immunology 2006, 176: 2105-2113. PMID: 16455966, DOI: 10.4049/jimmunol.176.4.2105.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAntigens, SurfaceBase SequenceCD28 AntigensCell NucleusCells, CulturedCytokinesCytoplasmELAV ProteinsELAV-Like Protein 1HumansLymphocyte ActivationLymphocyte Function-Associated Antigen-1Molecular Sequence DataRNA StabilityRNA, MessengerRNA, Small InterferingRNA-Binding ProteinsT-LymphocytesConceptsNuclear exportAU-rich element (ARE) sequenceMRNA stabilizationClass II AU-rich elementsT cell activationAU-rich elementsLymphokine gene expressionRapid nuclearRegulated processIntegrin engagementCell activationMRNA reporterRNA interferenceHuR functionIntegrin LFA-1MRNA stabilityGene expressionProtein productionHuman peripheral T cellsCytoplasmic translocationGM-CSF mRNAElement sequencesProtein HuRHuR levelsLFA-1
2004
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
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, MessengerRNA, Small NuclearRNA, ViralRNA-Binding ProteinsT-LymphocytesConceptsAU-rich elementsSmall nuclear RNAHSURs 1Herpesvirus saimiriNuclear RNAMRNA decay pathwayMarmoset T cellsHSUR 1HnRNP DPosttranscriptional regulationHost mRNAsHost proteinsMicroarray analysisUnknown functionProtein tristetraprolinVivo interactionDecay pathwaysHSURsMRNARNAMRNA levelsT cellsProteinCellsPathway
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 region
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 transportMRNAAUUUA Sequences Direct mRNA Deadenylation Uncoupled from Decay during Xenopus Early Development
Voeltz G, Steitz J. AUUUA Sequences Direct mRNA Deadenylation Uncoupled from Decay during Xenopus Early Development. Molecular And Cellular Biology 1998, 18: 7537-7545. PMID: 9819439, PMCID: PMC109334, DOI: 10.1128/mcb.18.12.7537.Peer-Reviewed Original ResearchConceptsAU-rich elementsXenopus early developmentGranulocyte-macrophage colony-stimulating factor (GM-CSF) geneUntranslated region sequencesHuman granulocyte-macrophage colony-stimulating factor geneChimeric mRNAMid-blastula transitionEarly developmentColony-stimulating factor geneRNA deadenylationMRNA decayRapid deadenylationMRNA deadenylationDeadenylation activityDeadenylationFactor genesRegion sequencesEgg activationAUUUAC-MycMature eggsXenopus oocytesMRNAOocytesXenopus
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