Search results for "nucleus"

showing 10 items of 1803 documents

Insulin-like growth factor 1 differentially regulates estrogen receptor-dependent transcription at estrogen response element and AP-1 sites in breast…

2007

Cross-talk between insulin-like growth factor 1 (IGF-1) and estrogen receptor alpha (ER) regulates gene expression in breast cancer cells, but the underlying mechanisms remain unclear. Here, we studied how 17-beta-estradiol (E2) and IGF-1 affect ER transcriptional machinery in MCF-7 cells. E2 treatment stimulated ER loading on the estrogen response element (ERE) in the pS2 promoter and on the AP-1 motif in the cyclin D1 promoter. On ERE, similar amounts of liganded ER were found at 1-24-h time points, whereas on AP-1, ER binding fluctuated over time. At 1 h, liganded ER was recruited to ERE together with histone acetyltransferases SRC-1 and p300, ubiquitin ligase E6-AP, histone methyltransf…

Transcription GeneticActive Transport Cell NucleusEstrogen receptorBreast NeoplasmsLigandsResponse ElementsBiochemistryCyclin D1Cell Line TumorHumansCyclin D1RNA MessengerInsulin-Like Growth Factor IHistone H3 acetylationMolecular BiologyHormone response elementbiologyEstradiolTumor Suppressor ProteinsEstrogen Receptor alphaCell BiologyUbiquitin ligaseCell biologyUp-RegulationTranscription Factor AP-1Histone methyltransferasebiology.proteinCancer researchMdm2Trefoil Factor-1Estrogen receptor alphahormones hormone substitutes and hormone antagonistsThe Journal of biological chemistry
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Cellular Inhibitor of Apoptosis Protein-1 (cIAP1) Can Regulate E2F1 Transcription Factor-mediated Control of Cyclin Transcription

2011

International audience; The inhibitor of apoptosis protein cIAP1 (cellular inhibitor of apoptosis protein-1) is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-B signaling pathways in the cytoplasm. However, in some primary cells and tumor cell lines, cIAP1 is expressed in the nucleus, and its nuclear function remains poorly understood. Here, we show that the N-terminal part of cIAP1 directly interacts with the DNA binding domain of the E2F1 transcription factor. cIAP1 dramatically increases the transcriptional activity of E2F1 on synthetic and CCNE promoters. This function is not conserved for cIAP2 and XIAP, which are cytoplasmic proteins. Chromatin immunoprec…

Transcription GeneticCellular differentiation[SDV]Life Sciences [q-bio]Cyclin ACyclin A[SDV.BC]Life Sciences [q-bio]/Cellular BiologyResponse ElementsInhibitor of apoptosisBiochemistryInhibitor of Apoptosis ProteinsMice03 medical and health sciences0302 clinical medicineCyclin EAnimalsHumansE2F1Gene SilencingE2F[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular BiologyCell Proliferation030304 developmental biologyCell Nucleus0303 health sciencesbiologyE2F1 Transcription FactorCell BiologyCell cycleMolecular biologyProtein Structure Tertiary3. Good healthCell biology[SDV] Life Sciences [q-bio]030220 oncology & carcinogenesisbiology.proteinbiological phenomena cell phenomena and immunityChromatin immunoprecipitationE2F1 Transcription FactorHeLa Cells
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Nuclear aggregation of olfactory receptor genes governs their monogenic expression.

2012

SummaryGene positioning and regulation of nuclear architecture are thought to influence gene expression. Here, we show that, in mouse olfactory neurons, silent olfactory receptor (OR) genes from different chromosomes converge in a small number of heterochromatic foci. These foci are OR exclusive and form in a cell-type-specific and differentiation-dependent manner. The aggregation of OR genes is developmentally synchronous with the downregulation of lamin b receptor (LBR) and can be reversed by ectopic expression of LBR in mature olfactory neurons. LBR-induced reorganization of nuclear architecture and disruption of OR aggregates perturbs the singularity of OR transcription and disrupts the…

Transcription GeneticCytoplasmic and NuclearChromosomal Proteins Non-HistoneDown-RegulationReceptors Cytoplasmic and NuclearLamin B receptorBiologyReceptors OdorantMedical and Health SciencesGeneral Biochemistry Genetics and Molecular BiologyFluorescenceOlfactory Receptor NeuronsArticle03 medical and health sciencesMice0302 clinical medicineDownregulation and upregulationGeneticTranscription (biology)HeterochromatinGene expressionReceptorsmedicineGeneticsAnimalsGeneIn Situ HybridizationIn Situ Hybridization Fluorescence030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesOlfactory receptorBiochemistry Genetics and Molecular Biology(all)Neurosciencesta1182Non-HistoneBiological SciencesCell biologyChromosomal Proteinsmedicine.anatomical_structureOdorantGene Expression RegulationEctopic expressionTranscription030217 neurology & neurosurgeryDevelopmental BiologyCell
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Energy requirement and kinetics of transport of poly(A)-free histone mRNA compared to poly(A)-rich mRNA from isolated L-cell nuclei.

1989

ATP-promoted efflux of poly(A)-rich RNA from isolated nuclei of prelabeled mouse lymphoma L5178y cells has an activation energy of 51.5 kJ/mol, similar to that found for the nuclear envelope nucleoside triphosphatase (48.1 kJ/mol) assumed to be involved in mediating nucleocytoplasmic transport of at least some RNA. Here we show that efflux of two specific poly(A)-rich mRNAs (actin and beta-tubulin) from isolated L-cell nuclei is almost totally dependent on the presence of ATP, while efflux of poly(A)-free histone mRNA (H4, H2B, and H1) also occurs to a marked extent in the absence of this nucleotide. Measurements of temperature dependence of transport rate revealed an activation energy of 5…

Transcription GeneticNuclear EnvelopeRNA transportBiochemistryHistonesMiceAnimalsNucleotideRNA MessengerBinding siteLeukemia L5178Actinchemistry.chemical_classificationCell NucleusMessenger RNALeukemia ExperimentalbiologyRNANucleic Acid HybridizationRibonucleotidesBlotting NorthernMolecular biologyKineticsHistoneEnzymechemistrybiology.proteinEnergy MetabolismPoly APlasmidsEuropean journal of biochemistry
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Transcriptional Activity and Nuclear Localization of Cabut, the Drosophila Ortholog of Vertebrate TGF-β-Inducible Early-Response Gene (TIEG) Proteins

2011

Background Cabut (Cbt) is a C2H2-class zinc finger transcription factor involved in embryonic dorsal closure, epithelial regeneration and other developmental processes in Drosophila melanogaster. Cbt orthologs have been identified in other Drosophila species and insects as well as in vertebrates. Indeed, Cbt is the Drosophila ortholog of the group of vertebrate proteins encoded by the TGF-s-inducible early-response genes (TIEGs), which belong to Sp1-like/Kruppel-like family of transcription factors. Several functional domains involved in transcriptional control and subcellular localization have been identified in the vertebrate TIEGs. However, little is known of whether these domains and fu…

Transcription GeneticNuclear Localization SignalsActive Transport Cell Nucleuslcsh:MedicineGene ExpressionBiochemistrybehavioral disciplines and activities03 medical and health sciencesModel Organisms0302 clinical medicineTransforming Growth Factor betaMolecular Cell Biologymental disordersGeneticsTranscriptional regulationAnimalsDrosophila Proteinslcsh:ScienceBiology030304 developmental biologyGeneticsZinc finger transcription factor0303 health sciencesMultidisciplinarybiologySchneider 2 cellslcsh:RfungiProteinsAnimal Modelsbiology.organism_classificationFusion proteinCellular StructuresDorsal closure3. Good healthRepressor ProteinsDrosophila melanogasterGene Expression RegulationVertebrateslcsh:QDrosophila melanogaster030217 neurology & neurosurgeryDrosophila ProteinNuclear localization sequenceTranscription FactorsResearch ArticleDevelopmental BiologyPLoS ONE
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Rapid nucleus-scale reorganization of chromatin in neurons enables transcriptional adaptation for memory consolidation

2020

AbstractThe interphase nucleus is functionally organized in active and repressed territories defining the transcriptional status of the cell. However, it remains poorly understood how the nuclear architecture of neurons adapts in response to behaviorally relevant stimuli that trigger fast alterations in gene expression patterns. Imaging of fluorescently tagged nucleosomes revealed that pharmacological manipulation of neuronal activity in vitro and auditory cued fear conditioning in vivo induce nucleus-scale restructuring of chromatin within minutes. Furthermore, the acquisition of auditory fear memory is impaired after infusion of a drug into auditory cortex which blocks chromatin reorganiz…

Transcription GeneticPhysiologySensory PhysiologyGene ExpressionSocial SciencesMiceCognitionLearning and MemoryAnimal CellsBehavioral ConditioningMedicine and Health SciencesPsychologyPremovement neuronal activityFear conditioningNeuronsMultidisciplinaryChromosome BiologyQRBrainAnimal ModelsAdaptation PhysiologicalChromatinSensory SystemsChromatinIn Vivo ImagingHistonemedicine.anatomical_structureAuditory SystemExperimental Organism SystemsMedicineEpigeneticsMemory consolidationCellular TypesAnatomyResearch ArticleImaging TechniquesScienceMouse ModelsBiologyResearch and Analysis MethodsAuditory cortexModel OrganismsMemoryFluorescence ImagingGeneticsmedicineAnimalsNucleosomeMemory ConsolidationCell NucleusAuditory CortexBehaviorBiology and Life SciencesCell BiologyCellular NeuroscienceAnimal Studiesbiology.proteinCognitive ScienceFear ConditioningNeuroscienceNucleusNeuroscience
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Estrogens increase transcription of the human endothelial NO synthase gene: analysis of the transcription factors involved.

1998

Abstract —Estrogens have been found to reduce the incidence of cardiovascular disease that has been ascribed in part to an increased expression and/or activity of the vasoprotective endothelial NO synthase (NOS III). Some reports have shown that the level of expression of this constitutive enzyme can be upregulated by estrogens. The current study investigates the molecular mechanism of the NOS III upregulation in human endothelial EA.hy 926 cells. Incubation of EA.hy 926 cells with 17β-estradiol or the more stable 17α-ethinyl estradiol enhanced NOS III mRNA and protein expression up to 1.8-fold, without changing the stability of the NOS III mRNA. There was no enhancement of NOS III mRNA af…

Transcription Geneticmedicine.drug_classBiologyEthinyl EstradiolTransfectionCell LineDownregulation and upregulationDrug StabilityEstradiol CongenersTranscription (biology)Consensus SequenceInternal MedicinemedicineHumansRNA MessengerPromoter Regions GeneticTranscription factorCell NucleusSp1 transcription factorMessenger RNABase SequenceEstradiolTissue ExtractsTransfectionDNAMolecular biologyEndothelial stem cellIsoenzymesEstrogenEndothelium VascularNitric Oxide Synthasehormones hormone substitutes and hormone antagonistsTranscription FactorsHypertension (Dallas, Tex. : 1979)
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Mechanism of leptin expression in breast cancer cells: role of hypoxia-inducible factor-1α

2007

We reported previously that the obesity hormone leptin is overexpressed in breast cancer biopsies. Here, we investigated molecular mechanisms involved in this process, focusing on conditions that are associated with obesity, that is, hyperinsulinemia and induction of hypoxia. By using quantitative real-time PCR, immunofluorescent detection of proteins and enzyme-linked immunosorbent assays, we found that treatment of MCF-7 breast cancer cells with high doses of insulin or the hypoxia-mimetic agent CoCl2, or culturing the cells under hypoxic conditions significantly increased the expression of leptin mRNA and protein. Notably, the greatest leptin mRNA and protein expression were observed und…

Transcriptional ActivationCancer Researchmedicine.medical_specialtyActive Transport Cell NucleusBreast NeoplasmsBiologymedicine.disease_causeleptinbreast cancerInternal medicineCoactivatorGene expressionTumor Cells CulturedGeneticsmedicineHumansInsulinHIFp300-CBP Transcription FactorsPromoter Regions GeneticMolecular BiologyCell NucleusRegulation of gene expressionBinding SitesLeptin receptorLeptinPromoterCobaltHypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaGene Expression Regulation NeoplasticEndocrinologyhyperinsulinemiaCarcinogenesisChromatin immunoprecipitationhormones hormone substitutes and hormone antagonistsProtein BindingOncogene
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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery

2004

12 páginas, 7 figuras, 1 tabla. Material suplementario en: https://doi.org/10.1016/S0092-8674(03)01025-0. The SUS1 sequences have been deposited in GenBank with the accession number AY278445.

Transcriptional ActivationNucleocytoplasmic Transport ProteinsDNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataActive Transport Cell NucleusPorinsRNA polymerase IIBiologyGeneral Biochemistry Genetics and Molecular BiologyFungal ProteinsTranscription (biology)AcetyltransferasesGene Expression Regulation FungalYeastsGene expressionGenes RegulatorTranscriptional regulationAmino Acid SequenceRNA MessengerNuclear proteinPromoter Regions GeneticHistone AcetyltransferasesRegulation of gene expressionCell NucleusBase SequenceBiochemistry Genetics and Molecular Biology(all)Nuclear ProteinsRNA-Binding ProteinsMolecular biologyCell biologySAGA complexRibonucleoproteinsbiology.proteinNuclear PoreGenes LethalChromatin immunoprecipitation
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Yeast karyopherin Kap95 is required for cell cycle progression at Start

2010

Abstract Background The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. Results When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel r…

Transcriptional ActivationSaccharomyces cerevisiae ProteinsNuclear Localization SignalsActive Transport Cell NucleusSaccharomyces cerevisiaeImportinBiologylcsh:QH573-671Transcription factorCells CulturedKaryopherinCell Nucleuschemistry.chemical_classificationlcsh:CytologyCell CycleCell BiologyCell cyclebeta KaryopherinsSubcellular localizationCell biologyDNA-Binding ProteinschemistryCytoplasmMutationTranscription Initiation SiteNuclear transportNuclear localization sequenceProtein BindingTranscription FactorsResearch ArticleBMC Cell Biology
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