Search results for "Nuclear transport"

showing 6 items of 26 documents

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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Cytoplasmic Parvovirus Capsids Recruit Importin Beta for Nuclear Delivery

2019

Parvoviruses are an important platform for gene and cancer therapy. Their cell entry and the following steps, including nuclear import, are inefficient, limiting their use in therapeutic applications. Two models exist on parvoviral nuclear entry: the classical import of the viral capsid using nuclear transport receptors of the importin (karyopherin) family or the direct attachment of the capsid to the nuclear pore complex leading to the local disintegration of the nuclear envelope. Here, by laser scanning confocal microscopy and in situ proximity ligation analyses combined with coimmunoprecipitation, we show that infection requires importin β-mediated access to the nuclear pore complex and …

alpha KaryopherinsCytoplasmNuclear EnvelopevirusesImmunologyActive Transport Cell NucleusImportinKaryopherinsBiologyVirus ReplicationMicrobiologyCell LineParvoviridae InfectionsParvovirus03 medical and health sciencesCapsidCytosolViral entryVirologyAnimalsNuclear pore030304 developmental biologyKaryopherinCell Nucleuschemistry.chemical_classification0303 health sciencesNucleoplasm030302 biochemistry & molecular biologyVirus Internalizationbeta KaryopherinsVirus-Cell InteractionsCell biologychemistryCytoplasmInsect ScienceNuclear PoreCapsid ProteinsNucleoporinNuclear transportJournal of Virology
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The effect of nanoparticle size and NLS density on nuclear targeting in cancer and normal cells; impaired nuclear import and aberrant nanoparticle in…

2017

The cell nucleus is an interesting target in many diseases with particular interest in cancer. Previously, nuclear targeted small and large chitosan nanoparticles (S-NPs≈25nm, and L-NPs≈150nm respectively), modified with low, intermediate and high densities of NLS (L-NLS, I-NLS and H-NLS) were developed and assessed in L929 fibroblasts. However, to evade apoptosis and stimulate tumor growth cancer cells are capable of manipulating the nuclear-cytoplasmic transport on many levels, making NPs that are capable of nuclear targeting in normal cells incapable of doing so in cancer. For such reason, here, the nuclear delivery efficiency of S-NPs and L-NPs was assessed as a function of their NLS de…

inorganic chemicals0301 basic medicineNuclear Localization SignalsPharmaceutical Science02 engineering and technologyImportinBiologyenvironment and public healthCell Line03 medical and health sciencesCell Line TumormedicineHumansNLSParticle SizeCells Culturedhealth care economics and organizationsChitosanHEK 293 cellstechnology industry and agricultureBiological TransportGliomaFibroblastsrespiratory system021001 nanoscience & nanotechnologyVirologyCell biologyCell nucleus030104 developmental biologymedicine.anatomical_structureApoptosisCancer cellNanoparticlesNuclear transport0210 nano-technologyNuclear localization sequenceJournal of Controlled Release
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The cell nucleus. A study in Burgundy

2019

ABSTRACT Wilhelm Bernhard’s revolutionary microscopy techniques helped him put forward the hypothesis of specialized compartmentalization of the nucleus. He also described for the first time the nuclear bodies and peri-chromatin fibrils, and demonstrated that these granules contain an RNA component. The tradition of biennial workshops, named after this great scientist, continues, and this year it took place in the heart of Burgundy, in Dijon, France (May 20–24, 2019, organized by INSERM UMR1231, UBFC), where well-fed participants emphasized the importance of viewing the cell nucleus as a hub of specialized colloidal compartments that orchestrate replication, transcription and nuclear transp…

lcsh:QH426-470media_common.quotation_subjectPhase separationArt history03 medical and health sciencesNeoplasmsmedicineAnimalsHumanslcsh:QH573-671nucleolusNuclear pore030304 developmental biologymedia_commonCell Nucleus0303 health scienceslcsh:Cytologynuclear pores030302 biochemistry & molecular biologyCell BiologyArtWilhelm Bernhard Workshop 2019lcsh:GeneticsMicroscopy ElectronCell nucleusmedicine.anatomical_structurelaminsRNANuclear transportNucleusLaminNucleus
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Import and impact : characterization of parvovirus-nucleus interactions

2016

tumakuljetusreseptoritviruksetkromatinisaatiomodification of nuclear architecturetumahuokosetcanine parvoviruspromotersnuclear transportDNApromoottoritinfektiotchromatinizationnuclear pore complextumaproteiinitparvovirukset
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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