Search results for "nucleus"

showing 10 items of 1803 documents

Cell Cycle Activation of the Swi6p Transcription Factor Is Linked to Nucleocytoplasmic Shuttling

2003

The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in the regulation of cell division. In the present work, we have characterized the function of the karyopherin Msn5p in the control of the cell cycle of Saccharomyces cerevisiae. Phenotypic analysis of the msn5 mutant revealed an increase in cell size and a functional interaction between Msn5p and the cell cycle transcription factor SBF (composed of the Swi4p and Swi6p proteins), indicating that Msn5p is involved in Start control. In fact, we have shown that the level of Cln2p protein is drastically reduced in an msn5 mutant. The effect on CLN2 expression is mediated at a transcriptional …

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticCell divisionChromosomal Proteins Non-HistoneActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyDNA-binding proteinCyclinsGene Expression Regulation FungalmedicineCell Growth and DevelopmentMolecular BiologyTranscription factorKaryopherinCell Nucleuschemistry.chemical_classificationCell CycleCell BiologyCell cycleSubcellular localizationCell biologyDNA-Binding ProteinsCell nucleusmedicine.anatomical_structurechemistryCytoplasmMutationCarrier ProteinsTranscription FactorsMolecular and Cellular Biology
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Gene expression is circular: factors for mRNA degradation also foster mRNA synthesis.

2013

SummaryMaintaining proper mRNA levels is a key aspect in the regulation of gene expression. The balance between mRNA synthesis and decay determines these levels. We demonstrate that most yeast mRNAs are degraded by the cytoplasmic 5′-to-3′ pathway (the “decaysome”), as proposed previously. Unexpectedly, the level of these mRNAs is highly robust to perturbations in this major pathway because defects in various decaysome components lead to transcription downregulation. Moreover, these components shuttle between the cytoplasm and the nucleus, in a manner dependent on proper mRNA degradation. In the nucleus, they associate with chromatin—preferentially ∼30 bp upstream of transcription start-sit…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticRNA StabilityGenes FungalRNA polymerase IIRNA-binding proteinSaccharomyces cerevisiaeGenètica molecularGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesGene Expression ProcessTranscription (biology)Gene Expression Regulation FungalGene expressionP-bodiesmedicineRNA Messenger030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesbiologyBiochemistry Genetics and Molecular Biology(all)030302 biochemistry & molecular biologyRNA-Binding ProteinsRNA FungalMolecular biologyCell biologyCell nucleusmedicine.anatomical_structureExoribonucleasesbiology.proteinRNARNA Polymerase IICell
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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Nuclear and Cytoplasmic Soluble Proteins Extraction from a Small Quantity of Drosophila’s Whole Larvae and Tissues

2015

The identification and study of protein’s function in several model organisms is carried out using both nuclear and cytoplasmic extracts. For a long time, Drosophila’s embryos have represented the main source for protein extractions, although in the last year, the importance of collecting proteins extracts also from larval tissues has also been understood. Here we report a very simple protocol, improved by a previously developed method, to produce in a single extraction both highly stable nuclear and cytoplasmic protein extracts from a small quantity of whole Drosophila’s larvae or tissues, suitable for biochemical analyses like co-immunoprecipitation.

Cytoplasmanimal structuresved/biology.organism_classification_rank.speciesBiologyCell FractionationCatalysislcsh:ChemistryInorganic ChemistryCytoplasmic proteinBotanyTechnical NoteAnimalsDrosophila ProteinsPhysical and Theoretical ChemistryModel organismlcsh:QH301-705.5Molecular BiologyDrosophilaSpectroscopyCell NucleusLarvaved/biologyOrganic ChemistryExtraction (chemistry)fungiproteins extractionEmbryoGeneral Medicinebiology.organism_classificationhnRNPsComputer Science ApplicationsDrosophila melanogasterlcsh:Biology (General)lcsh:QD1-999BiochemistryCytoplasmLarvaDrosophilaFunction (biology)International Journal of Molecular Sciences
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A comparison of cytoplasmic and nuclear estradiol and progesterone receptors in human fallopian tube and endometrial tissue

1981

Quantitative and qualitative aspects of the in vitro binding of 3 H-estradiol and 3 H-progesterone to receptor components from human endometrium and fallopian tube cytoplasmic and nuclear fractions were studied. The steroid binding macromolecules formed in vitro could be extracted from nuclei by 0.4M KCl and detected by glycerol gradient centrifugation. Both estradiol- and progesterone-binding compounds formed only one peak (under high ionic strength conditions) with a sedimentation coefficient of about 4-5S. The number of cytoplasmic and nuclear binding sites for both estradiol and R5020 varied dramatically throughout the menstrual cycle: the estradiol and progesterone receptor concentrati…

Cytoplasmmedicine.medical_specialtymedia_common.quotation_subjectmedicine.medical_treatmentBiologyPromegestoneSteroidInfundibulumEndometriumInternal medicineProgesterone receptorFollicular phasemedicineHumansTissue DistributionReceptorFallopian TubesProgesteroneMenstrual cyclemedia_commonCell NucleusEstradiolObstetrics and GynecologyMenstruationCytosolEndocrinologymedicine.anatomical_structureReceptors EstrogenReproductive MedicineFemaleReceptors Progesteronehormones hormone substitutes and hormone antagonistsFallopian tubeFertility and Sterility
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Activation of the human immune system via toll-like receptors by the oncolytic parvovirus H-1.

2012

This study aimed to investigate the function of toll-like receptors (TLRs) during oncolytic parvovirus H-1 (H-1PV)-induced human immune responses. First, the role of TLRs in the activation of the NFκB transcription factor was characterized; second, the immunologic effects of H-1PV-induced tumor cell lysates (TCL) on human antitumor immune responses were evaluated. A human ex vivo model was used to study immune responses with dendritic cells (DCs). Human embryonic kidney cells (HEK293) transfected to stably express TLRs were used as potential human DC equivalents to further investigate the role of specific TLRs during immune activation. TLR3 and TLR9 were activated by H-1PV infection, which …

Cytotoxicity ImmunologicH-1 parvovirusCancer ResearchCytoplasmParvovirus H-1chemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayBiologyKidneyProinflammatory cytokineParvoviridae InfectionsImmune systemTumor Cells CulturedHumansMelanomaCells CulturedCell NucleusOncolytic VirotherapyTumor Necrosis Factor-alphaToll-Like ReceptorsNF-kappa BDendritic CellsAcquired immune systemFlow CytometryCell biologyOncolytic virusOncolytic VirusesOncologyImmune SystemImmunologyTLR3CytokinesTumor necrosis factor alphaSignal transductionSignal TransductionInternational journal of cancer
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Nuclear Localization of PTEN by a Ran-dependent Mechanism Enhances Apoptosis: Involvement of an N-Terminal Nuclear Localization Domain and Multiple N…

2006

The targeting of the tumor suppressor PTEN protein to distinct subcellular compartments is a major regulatory mechanism of PTEN function, by controlling its access to substrates and effector proteins. Here, we investigated the molecular basis and functional consequences of PTEN nuclear/cytoplasmic distribution. PTEN accumulated in the nucleus of cells treated with apoptotic stimuli. Nuclear accumulation of PTEN was enhanced by mutations targeting motifs in distinct PTEN domains, and it was dependent on an N-terminal nuclear localization domain. Coexpression of a dominant negative Ran GTPase protein blocked PTEN accumulation in the nucleus, which was also affected by coexpression of importin…

Cèl·lulesAmino Acid MotifsMolecular Sequence DataNuclear Localization SignalsApoptosisBiologyModels BiologicalCatalysislaw.inventionMicelawChlorocebus aethiopsmedicineAnimalsHumansPTENAmino Acid SequenceProteïnes supressores de tumorsMolecular BiologyCells CulturedSequence DeletionCell NucleusCOS cellsEffectorPTEN Phosphohydrolase3T3 CellsArticlesCell BiologyProtein Structure TertiaryRatsTransport proteinProtein TransportCell nucleusran GTP-Binding Proteinmedicine.anatomical_structureCOS CellsRanbiology.proteinCancer researchSuppressorNuclear localization sequenceHeLa CellsMolecular Biology of the Cell
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Role of glutathione in cell nucleus

2010

Cells with high proliferation rate have high glutathione levels. This typical feature of cancer cells is viewed usually as a defence mechanism against ionizing radiation or chemotherapy. Efforts have been made in order to decrease cellular glutathione levels in tumours as a necessary pre-treatment for cancer therapy. However, very few reports have considered cellular glutathione as a physiological tool for cells to proliferate and that most of this high glutathione levels were located in the nucleus. The role of nuclear glutathione in cell physiology has become more important in the last years. This review summarizes new findings that point to the nuclear reduced status as an environment th…

DNA RepairDNA repairBiochemistryHistonesProtein Carbonylationchemistry.chemical_compoundHeterochromatinmedicineAnimalsHumansNuclear proteinTelomeraseCell NucleusbiologyCell CycleNuclear ProteinsDNAGeneral MedicineGlutathioneCell cycleGlutathioneChromatinCell biologyHistonemedicine.anatomical_structurechemistryCancer cellbiology.proteinOxidation-ReductionProtein Processing Post-TranslationalNucleusFree Radical Research
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UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles

2006

The DNA glycosylase hOGG1 initiates base excision repair (BER) of oxidised purines in cellular DNA. Using confocal microscopy and biochemical cell fractionation experiments we show that, upon UVA irradiation of human cells, hOGG1 is recruited from a soluble nucleoplasmic localisation to the nuclear matrix. More specifically, after irradiation, hOGG1 forms foci colocalising with the nuclear speckles, organelles that are interspersed between chromatin domains and that have been associated with transcription and RNA-splicing processes. The use of mutant forms of hOGG1 unable to bind the substrate showed that relocalisation of hOGG1 does not depend on the recognition of the DNA lesion by the en…

DNA RepairTranscription GeneticUltraviolet RaysDNA repairRecombinant Fusion ProteinsGreen Fluorescent ProteinsFluorescent Antibody TechniqueBiologyDNA GlycosylasesSubstrate Specificitychemistry.chemical_compoundDNA Repair ProteinDNA-(Apurinic or Apyrimidinic Site) LyaseHumansCell NucleusGuanosineBiological TransportCell BiologyBase excision repairNuclear matrixMolecular biologyChromatinCell biologychemistryDNA glycosylaseCell fractionationReactive Oxygen SpeciesDNAHeLa CellsJournal of Cell Science
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