Search results for "Protein transport"

showing 10 items of 197 documents

Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2

2002

AbstractNuclear domains (ND) 10 are associated with proteins implicated in transcriptional regulation, growth suppression, and apoptosis. We now show that the minor capsid protein L2 of human papillomavirus (HPV) type 33 induces a reorganization of ND10-associated proteins. Whereas the promyelocytic leukemia protein, the major structural component of ND10, was unaffected by L2, Sp100 was released from ND10 upon L2 expression. The total cellular amount of Sp100, but not of Sp100 mRNA, decreased significantly, suggesting degradation of Sp100. Proteasome inhibitors induced the dispersal of Sp100 and inhibited the nuclear translocation of L2. In contrast to Sp100, Daxx was recruited to ND10 by …

Co-Repressor ProteinsImmunoprecipitationFluorescent Antibody TechniqueVaccinia virusPromyelocytic Leukemia ProteinAutoantigenspapillomavirusCell LinePromyelocytic leukemia proteinCapsidDeath-associated protein 6DaxxVirologyHumansSp100RNA MessengerAdaptor Proteins Signal TransducingCell NucleusRecombination GeneticbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsND10Signal transducing adaptor proteinAntigens NuclearOncogene Proteins ViralL2biochemical phenomena metabolism and nutritionBlotting NorthernMolecular biologyNeoplasm ProteinsTransport proteinCell biologyProtein TransportProteasomeCapsidbiology.proteinRNACapsid ProteinsFemaleCarrier ProteinsCo-Repressor ProteinsMolecular ChaperonesTranscription FactorsVirology
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Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.

2004

The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…

CoatPhysiologyAmino Acid MotifsArabidopsisReceptors Cytoplasmic and NuclearPlant ScienceBiologyCoat Protein Complex ICytosolAnimalsCOPIIBinding SitesVesicular-tubular clusterArabidopsis ProteinsCell BiologyGeneral MedicineCOPIPlant cellIn vitroPeptide FragmentsCell biologyRatsCytosolProtein TransportRat liverCOP-Coated VesiclesProtein BindingSignal TransductionPlantcell physiology
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Myc Promoter-Binding Protein-1 (MBP-1) Is a Novel Potential Prognostic Marker in Invasive Ductal Breast Carcinoma

2010

BackgroundAlpha-enolase is a glycolytic enzyme that catalyses the formation of phosphoenolpyruvate in the cell cytoplasm. α-Enolase and the predominantly nuclear Myc promoter-binding protein-1 (MBP-1) originate from a single gene through the alternative use of translational starting sites. MBP-1 binds to the P2 c-myc promoter and competes with TATA-box binding protein (TBP) to suppress gene transcription. Although several studies have shown an antiproliferative effect of MBP-1 overexpression on several human cancer cells, to date detailed observations of α-enolase and MBP-1 relative expression in primary tumors versus normal tissues and their correlation with clinicopathological features ha…

CytoplasmAlpha-enolasePROGRESSIONAged 80 and overRegulation of gene expressionMultidisciplinaryQRGenetics and Genomics/Gene ExpressionMiddle AgedPrognosisPathology/Molecular PathologyNUDE-MICETransport proteinCarcinoma DuctalDNA-Binding ProteinsGene Expression Regulation NeoplasticProtein Transportmedicine.anatomical_structureGLYCOLYTIC ENZYMEOncology/Breast CancerMedicineCELL LUNG-CANCER; ALPHA-ENOLASE; PROTEOMIC ANALYSIS; GLYCOLYTIC ENZYME; NUDE-MICE; GENE; IDENTIFICATION; PROGRESSION; EXPRESSION; METASTASESFemalePROTEOMIC ANALYSISEnolase MBP-1 Breast cancer ImmunohistochemistryResearch ArticleAdultEXPRESSIONScienceCELL LUNG-CANCERBreast NeoplasmsBiologyDNA-binding proteinBiomarkers TumormedicineHumansNeoplasm InvasivenessGeneAgedCell NucleusIDENTIFICATIONBinding proteinALPHA-ENOLASEGENEMolecular biologySettore BIO/18 - GeneticaCell nucleusMETASTASESCytoplasmPhosphopyruvate Hydratasebiology.proteinPLoS ONE
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Multifunctionality of F-rich nucleoporins

2020

Nucleoporins (Nups) represent a range of proteins most known for composing the macromolecular assembly of the nuclear pore complex (NPC). Among them, the family of intrinsically disordered proteins (IDPs) phenylalanine-glycine (FG) rich Nups, form the permeability barrier and coordinate the high-speed nucleocytoplasmic transport in a selective way. Those FG-Nups have been demonstrated to participate in various biological processes besides nucleocytoplasmic transport. The high number of accessible hydrophobic motifs of FG-Nups potentially gives rise to this multifunctionality, enabling them to form unique microenvironments. In this review, we discuss the multifunctionality of disordered and …

CytoplasmProtein FoldingDNA RepairPhenylalanineAmino Acid MotifsActive Transport Cell NucleusGlycineIntrinsically disordered proteinsBiochemistryArticle03 medical and health sciences0302 clinical medicineAnimalsHumansCell LineageCiliaNuclear pore030304 developmental biologyCell Nucleus0303 health sciencesChemistryNeurodegenerative DiseasesIntrinsically Disordered ProteinsNuclear Pore Complex ProteinsMacromolecular assemblyProtein TransportGene Expression RegulationNucleocytoplasmic TransportNuclear PoreBiophysicsNucleoporinHydrophobic and Hydrophilic Interactions030217 neurology & neurosurgeryBiological networkBiochemical Society Transactions
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Analysis of cytochrome C oxidase subunits III and IV expression in developing rat brain

2004

Abstract Cytochrome c oxidase (COX) complex is built up with both nucleus- and mitochondrion-encoded subunits. Biogenesis and assembly of the complex thus requires fine cross-talk between the two compartments. In order to shed light on the regulation of nuclear–mitochondrial interactions, we studied the expression of COXIII (mitochondrion-encoded) and COXIV (nucleus-encoded) in adult rat tissues and rat developing brain. We found that the levels of COXIV protein and mRNA are not linearly related, thus suggesting a post-transcriptional mode of regulation. In agreement with this observation, we report the presence of a protein that specifically binds to the 3′-untranslated region of COXIV mRN…

CytoplasmRNA-binding proteinProtein subunitBlotting WesternCOX IVRNA-binding proteinMitochondrionBiologyGene Expression Regulation EnzymologicElectron Transport Complex IVAnimalsCytochrome c oxidaseElectrophoresis Gel Two-DimensionalCOX III.RNA MessengerRNA Processing Post-TranscriptionalMessenger RNAGeneral NeuroscienceBrainProteinsRNABlotting NorthernMitochondriaRatsProtein TransportCytosolnucleus-mitochondrion cross-talkBiochemistryCytoplasmbiology.proteinNeuroscience
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Regulation of ribonucleotide reductase in response to iron deficiency

2011

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2–Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity, and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the re…

CytoplasmSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleoside Diphosphate ReductaseRNA StabilityProtein subunitSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiologyResponse ElementsArticleTristetraprolinGene Expression Regulation FungalRibonucleotide ReductasesHumansRNA MessengerMolecular BiologyTranscription factorCell NucleusDNA synthesisIntracellular Signaling Peptides and ProteinsFungal geneticsRNA-Binding ProteinsRNA FungalIron DeficienciesCell Biologybiology.organism_classificationDNA-Binding ProteinsRepressor ProteinsCheckpoint Kinase 2Protein SubunitsProtein TransportRibonucleotide reductaseBiochemistryCytoplasmTranscription Factors
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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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Cutting edge: priming of CTL by transcutaneous peptide immunization with imiquimod.

2005

Abstract CTL are important in combating cancer and viruses. Therefore, triggering the complete potential of CTL effector functions by new vaccination strategies will not only improve prophylaxis of tumor or virus-related diseases, but also open opportunities for effective therapeutic immunizations. Using transcutaneous immunization, we show that epicutaneous (e.c.)4 application of an ointment containing a CTL epitope and the TLR7 ligand imiquimod is highly effective in activating T cells in mice using TCR-transgenic CTL or in wild-type mice. Transcutaneous immunization-activated CTL mount a full-blown immune response against the target epitope characterized by proliferation, cytolytic activ…

Cytotoxicity ImmunologicAdoptive cell transferImmunologyReceptors Antigen T-CellPriming (immunology)Epitopes T-Lymphocytechemical and pharmacologic phenomenaImiquimodMice TransgenicAdministration CutaneousLymphocyte ActivationResting Phase Cell CycleEpitopeMiceImmune systemmedicineImmunology and AllergyAnimalsCells CulturedMice KnockoutImiquimodbusiness.industryTLR7VirologyAdoptive TransferVaccinationMice Inbred C57BLCTL*Protein TransportImmunologyVaccines SubunitAminoquinolinesLymph NodesbusinessSpleenmedicine.drugT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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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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