Search results for "nuclear envelope"

showing 10 items of 26 documents

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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Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells

1997

Many strains of Vibrio cholerae non-O1 and O1 El Tor that cause diarrhea do not harbor genes for a known secretogenic toxin. However, these strains usually elaborate a pore-forming toxin, hitherto characterized as a hemolysin and here designated V. cholerae cytolysin, whose action on intestinal cells has not yet been described. We report that V. cholerae cytolysin binds as a monomer to Intestine 407 cells and then assembles into detergent-stable oligomers that probably represent tetra- or pentamers. Oligomer formation is accompanied by generation of small transmembrane pores that allow rapid flux of K+ but not influx of Ca2+ or propidium iodide. Pore formation is followed by irreversible AT…

Nuclear EnvelopeImmunologymedicine.disease_causeMicrobiologyEl TorMicrobiologychemistry.chemical_compoundVibrionaceaemedicineHumansPropidium iodideVibrio choleraeCells CulturedIon TransportCell DeathbiologyCytotoxinsToxinCell MembraneHemolysinbiology.organism_classificationIntestinesInfectious DiseaseschemistryVibrio choleraeCell cultureParasitologyCytolysinResearch ArticleInfection and Immunity
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Proteins from rat liver cytosol which stimulate mRNA transport. Purification and interactions with the nuclear envelope mRNA translocation system.

1986

Two polysome-associated proteins with particular affinities for poly(A) have been purified from rat liver. These proteins stimulate the efflux of mRNA from isolated nuclei in conditions under which such efflux closely stimulates mRNA transport in vivo, and they are therefore considered as mRNA-transport-stimulatory proteins. Their interaction with the mRNA-translocation system in isolated nuclear envelopes has been studied. The results are generally consistent with the most recently proposed kinetic model of mRNA translocation. One protein, P58, has not been described previously. It inhibits the protein kinase that down-regulates the NTPase, it enhances the NTPase activity in both the prese…

MaleNucleocytoplasmic Transport ProteinsNuclear EnvelopeRNA-binding proteinBiologyBiochemistryCytosolPhosphoprotein PhosphatasesMRNA transportAnimalsRNA MessengerProtein kinase AMessenger RNANucleocytoplasmic Transport ProteinsRNARNA-Binding ProteinsBiological TransportRats Inbred StrainsNucleoside-TriphosphatasePhosphoric Monoester HydrolasesCell biologyRatsCytosolBiochemistryLiverPolyribosomesPhosphorylationCarrier ProteinsPoly AProtein KinasesEuropean journal of biochemistry
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Differential effect of insulin and epidermal growth factor on the mRNA translocation system and transport of specific poly(A+) mRNA and poly(A-) mRNA…

1990

The efficiency of efflux of rapidly labeled poly(A)-containing mRNA from isolated rat liver nuclei was found to be modulated by insulin and epidermal growth factor (EGF) in a biphasic but opposite way. At physiological concentrations (10 pM insulin and 1 pM EGF), maximal stimulation of the transport rate by insulin (to 137%) and maximal inhibition by EGF (to 69%) were obtained; at higher concentrations (greater than 100 pM and greater than 10 pM, respectively), the amount of poly(A)-containing mRNA released into the postnuclear supernatant was nearly identical with the level found in untreated nuclei (= 100%). Using mRNA entrapped into closed nuclear envelope (NE) vesicles as a model system…

MaleNuclear Envelopemedicine.medical_treatmentPhosphoprotein phosphatase activityBiologyBiochemistryDephosphorylationAdenosine TriphosphateEpidermal growth factormedicineCyclic AMPMRNA transportAnimalsInsulinRNA MessengerBinding sitePhosphorylationCyclic GMPCell NucleusMessenger RNAEpidermal Growth FactorInsulinBiological TransportRats Inbred StrainsBlotting NorthernNucleoside-TriphosphataseMolecular biologyPhosphoric Monoester HydrolasesRatsKineticsPhosphorylationPoly ABiochemistry
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Modulation of the nuclear-envelope nucleoside triphosphatase by poly(A)-rich mRNA and by microtubule protein.

1982

Nuclear envelopes contain a nucleoside triphosphatase which is thought to be involved in the supply of energy for nucleo-cytoplasmic RNA transport. This enzyme is stimulated most efficiently by poly(A) and to a lesser extent by poly(G) and poly(dT). Half-maximal stimulation of the enzyme from rat liver nuclei, which was associated with the poly(A)-specific endoribonuclease IV and was free from poly(A) polymerase and endoribonuclease V activity, was determined to occur at a concentration of 1.1 × 106 poly(A) molecules/nuclear ghost. Double-reciprocal plot analyses revealed a 2.8-fold stimulation of the enzyme by poly(A). Poly(A) in the hybrid form had no influence on the activity of the nucl…

MaleNuclear EnvelopeEndoribonucleaseRNA transportIn Vitro TechniquesBiochemistryPolydeoxyribonucleotidesTubulinAnimalsNucleotideRNA MessengerPolymerasechemistry.chemical_classificationMessenger RNAbiologyRNABiological TransportRats Inbred StrainsNucleoside-TriphosphataseEnzyme assayActinsPhosphoric Monoester HydrolasesRatsEnzyme ActivationTubulinchemistryBiochemistrybiology.proteinPoly APolyribonucleotidesEuropean journal of biochemistry
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Nuclear entry and egress of parvoviruses.

2022

Parvoviruses are small non-enveloped single-stranded DNA viruses, which depend on host cell nuclear transcriptional and replication machinery. After endosomal exposure of nuclear localization sequence and a phospholipase A2 domain on the capsid surface, and escape into the cytosol, parvovirus capsids enter the nucleus. Due to the small capsid diameter of 18–26 nm, intact capsids can potentially pass into the nucleus through nuclear pore complexes (NPCs). This might be facilitated by active nuclear import, but capsids may also follow an alternative entry pathway that includes activation of mitotic factors and local transient disruption of the nuclear envelope. The nuclear entry is followed b…

import and exportCell NucleusisäntäsolutviruksetparvovirusesNuclear Envelopenuclear pore complexesnucleusActive Transport Cell NucleusDNA Single-Strandednuclear envelopeVirus ReplicationMicrobiologyinfektiotParvovirusPhospholipasestumaNuclear PoreCapsid ProteinsMolecular BiologyparvoviruksetkapsidiMolecular microbiologyREFERENCES
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Age-dependent changes of nuclear envelope protein phosphokinase and protein phosphatase activities. Significance for altered nucleo-cytoplasmic mRNA …

1984

Nuclear envelopes are associated with a protein phosphokinase and a phosphoprotein phosphatase, whose activities are modulated by poly(A) in an opposite manner. The activities of these enzymes were determined in nuclear ghosts from liver and oviduct of quails of different age and of different hormone status. Under optimal conditions, kinase activity was found to increase in immature animals 8-fold in response to diethylstilbestrol; co-administration of progesterone had no marked effect on enzyme activity. After the initial burst, the activity of the enzyme increased only slightly during ageing. Two proteins present in nuclear ghosts of Mr 64 000 and of Mr 106 000 are phosphorylated during t…

medicine.medical_specialtyAgingNuclear Envelopemedicine.medical_treatmentPhosphataseOviductsQuailInternal medicinemedicinePhosphoprotein PhosphatasesAnimalsProtein phosphorylationRNA MessengerKinase activityPhosphorylationProtein kinase ADiethylstilbestrolProgesteronebiologyKinaseBiological TransportEnzyme assayMolecular WeightSteroid hormoneEndocrinologyLiverbiology.proteinPhosphorylationFemaleProtein KinasesDevelopmental BiologyMechanisms of ageing and development
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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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Compromised nuclear envelope integrity drives TREX1-dependent DNA damage and tumor cell invasion

2021

Although mutations leading to a compromised nuclear envelope cause diseases such as muscular dystrophies or accelerated aging, the consequences of mechanically induced nuclear envelope ruptures are less known. Here, we show that nuclear envelope ruptures induce DNA damage that promotes senescence in non-transformed cells and induces an invasive phenotype in human breast cancer cells. We find that the endoplasmic reticulum (ER)-associated exonuclease TREX1 translocates into the nucleus after nuclear envelope rupture and is required to induce DNA damage. Inside the mammary duct, cellular crowding leads to nuclear envelope ruptures that generate TREX1-dependent DNA damage, thereby driving the …

SenescenceExonucleaseDNA damageNuclear Envelope[SDV]Life Sciences [q-bio]Breast NeoplasmsBiologySettore MED/08 - Anatomia PatologicaGeneral Biochemistry Genetics and Molecular BiologyCell LineMicemedicineSettore MED/05 - Patologia ClinicaAnimalsHumansNeoplasm InvasivenessEpithelial–mesenchymal transitionCellular SenescenceEndoplasmic reticulumPhosphoproteinsXenograft Model Antitumor AssaysCell biology[SDV] Life Sciences [q-bio]medicine.anatomical_structureExodeoxyribonucleasesCancer cellProteolysisbiology.proteinTREX1 nuclear envelope rupture DNA damage mammary duct carcinoma tumor invasion senescence breast cancer cGAS confinement epithelial to mesenchymal transition Animals Breast Neoplasms Cell Line Cellular Senescence Collagen Disease Progression Exodeoxyribonucleases Female Humans Mice Neoplasm InvasivenessNuclear Envelope PhosphoproteinsProteolysis Xenograft Model Antitumor Assays DNA DamageDisease ProgressionFemaleCollagenNucleusExtracellular Matrix DegradationDNA Damage
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All-trans to 11-cis retinol isomerization in nuclear membrane fraction from bovine retinal pigment epithelium

1991

Abstract Isomerization of all-trans to 11-cis retinol has been studied in a membrane preparation from the nuclear fraction of bovine retinal pigment epithelium. When the nuclear membrane preparation deprived of endogenous retinoids is incubated with 4·5 μ m all-trans-retinol, the mean value calculated for the isomerase activity is 1·32 nmol 11-cis retinol formed hr−1 mg protein−1. Simultaneous formation of all-trans and 11-cis retinyl esters is also observed in the nuclear preparation. When assayed under the same experimental condition, RPE 150 000 g post-nuclear sediment shows about 70% of the isomerase activity found in the nuclear membrane fraction. Treatment of the nuclear membrane frac…

cis-trans-IsomerasesIsomerase activityNuclear EnvelopeDetergentsIsomeraseCellular and Molecular Neurosciencechemistry.chemical_compoundIsomerismChapsmedicineAnimalsBovine serum albuminNuclear membraneIsomerasesPigment Epithelium of EyeVitamin AChromatography High Pressure LiquidCell NucleusChromatographybiologyRetinolCholic AcidsSensory SystemsEnzyme assayOphthalmologyMembranemedicine.anatomical_structureSolubilityBiochemistrychemistrybiology.proteinCattleExperimental Eye Research
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