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, MessengerRNA-Binding ProteinsTetrahydrofolate 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 genes
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, MessengerRNA-Binding ProteinsSequence 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