Search results for "nuclear pore complex"

showing 10 items of 20 documents

Differential functions of calpain 1 during epithelial cell death and adipocyte differentiation in mammary gland involution

2014

Calpains become activated in the mammary gland early during weaning, cleaving several proteins located mainly in the cell membrane, but also in other organelles such as lysosomes, mitochondria and nuclei. By immunofluorescence and Western blot analysis, we have demonstrated the nuclear translocation of calpain-1 and calpain-2, together with the cleavage of several cytoplasmic nucleoporins in epithelial cells of the lobulo-alveolar compartment. In vivo and in vitro calpain inhibition prevented this nucleoporin degradation. In addition, calpain-1 was also present in the nucleus of non-epithelial mammary tissue cells, concomitant with adipocyte re-differentiation. Calpain-1 was internalized wi…

MaleCellular differentiationBiochemistryHistonesMicechemistry.chemical_compoundHistone H3Mammary Glands AnimalAdipocyteAdipocytesAnimalsLactationMolecular BiologyMammary gland involutionbiologyCalpainCell DifferentiationEpithelial CellsCalpainCell BiologyMolecular biologyNuclear Pore Complex ProteinsProtein TransportHistoneGene Expression Regulationchemistrybiology.proteinH3K4me3FemaleNucleoporinBiochemical Journal
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Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport

1988

The rate of energy-dependent nucleoside triphosphatase (NTPase)-mediated nucleocytoplasmic translocation of poly(A)-containing mRNA [poly(A)+mRNA] across the nuclear envelope is thought to be regulated by poly(A)-sensitive phosphorylation and dephosphorylation of nuclear-envelope protein. Studying the phosphorylation-related inhibition of the NTPase, we found that phosphorylation of one polypeptide of rat liver envelopes by endogenous NI- and NII-like protein kinase was particularly sensitive to poly(A). This polypeptide (106 kDa) was also phosphorylated by nuclear-envelope-bound Ca2+-activated and phospholipid-dependent protein kinase (protein kinase C). Activation of kinase C by tumour-pr…

MaleCytoplasmNuclear EnvelopeMitogen-activated protein kinase kinasePhosphatidylinositolsBiochemistryMAP2K7AnimalsRNA Messengerc-RafProtein kinase AMolecular BiologyProtein Kinase CProtein kinase CCell NucleusMembrane GlycoproteinsMAP kinase kinase kinasebiologyCyclin-dependent kinase 2Membrane ProteinsNuclear ProteinsBiological TransportRats Inbred StrainsCell BiologyMolecular biologyRatsNuclear Pore Complex ProteinsMicroscopy ElectronLiverBiochemistrybiology.proteinCyclin-dependent kinase 9PeptidesPoly AResearch ArticleBiochemical Journal
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The liquid state of FG-nucleoporins mimics permeability barrier properties of nuclear pore complexes

2019

Nuclear pore complexes form a permeability barrier in vivo that regulates nucleocytoplasmic transport. Here, the authors present a microfluidic device that couples rapid liquid–liquid phase separation of nucleoporins with direct optical interrogation. Freshly formed liquid nucleoporin droplets mimic permeability barrier properties of NPCs.

MicrofluidicsActive Transport Cell Nucleus48BiologyPermeability2303 medical and health sciences0302 clinical medicineReportmedicineMoleculeNuclear poreResearch Articles030304 developmental biology0303 health sciences36Cell Biology34Nuclear Pore Complex ProteinsCell nucleusmedicine.anatomical_structurePermeability (electromagnetism)Nucleocytoplasmic TransportBiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryThe Journal of Cell Biology
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Insights into mRNP biogenesis provided by new genetic interactions among export and transcription factors.

2012

Abstract Background The various steps of mRNP biogenesis (transcription, processing and export) are interconnected. It has been shown that the transcription machinery plays a pivotal role in mRNP assembly, since several mRNA export factors are recruited during transcription and physically interact with components of the transcription machinery. Although the shuttling DEAD-box protein Dbp5p is concentrated on the cytoplasmic fibrils of the NPC, previous studies demonstrated that it interacts physically and genetically with factors involved in transcription initiation. Results We investigated the effect of mutations affecting various components of the transcription initiation apparatus on the…

Nucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae Proteinslcsh:QH426-470MutantActive Transport Cell NucleusRNA-binding proteinRNA polymerase IISaccharomyces cerevisiaeDEAD-box RNA HelicasesTranscription (biology)GeneticsGenetics(clinical)RNA MessengerNuclear poreMex67pTranscription factorGenetics (clinical)AllelesDbp5pGeneticsmRNA exportbiologyGeneral transcription factorfungiNuclear ProteinsRNA-Binding Proteinslcsh:GeneticsRibonucleoproteinsMutationbiology.proteinNuclear PoreRNA Polymerase IINuclear Pore ComplexTranscriptionBiogenesisTranscription FactorsResearch ArticleBMC genetics
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Reorganization of Nuclear Pore Complexes and the Lamina in Late-Stage Parvovirus Infection

2015

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Parvovirus Canineanimal diseasesvirusesnuclear pore complexesImmunologyMicrobiologyParvoviridae InfectionsCapsidDogsVirologymedicineotorhinolaryngologic diseasesAnimalsDog DiseasesNuclear poreparvovovirusCell NucleusNuclear LaminaLamin Type BbiologyParvovirusParvovirus infectionCanine parvovirusLamin Type Abiology.organism_classificationmedicine.diseaseVirologyVirus-Cell InteractionsCell biologyNuclear Pore Complex ProteinsCell nucleusstomatognathic diseasesmedicine.anatomical_structureInsect ScienceNuclear PoreNuclear laminaNucleusLamin
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Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis

2013

The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes a protein required for the nuclear import of RNA pol II. Using protein affinity purification coupled to mass spectrometry, we identified interactions between Rtp1p and members of the R2TP complex. Rtp1p also interacts, to a different extent, with several RNA pol II subunits. The pattern of interactions is compatible with a role for Rtp1p as an assembly factor that participates in the formation of the Rpb2/Rpb3 subassembly complex and its bi…

Saccharomyces cerevisiae ProteinsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeKaryopherinsBiologyGene Expression Regulation FungalTranscriptional regulationRNA polymerase IProtein Interaction MapsMolecular BiologyRNA polymerase II holoenzymeR2TP complexGeneticsNuclear cap-binding protein complexArticlesCell BiologyPhosphoproteinsUp-RegulationCell biologyNuclear Pore Complex Proteinsbiology.proteinRNA Polymerase IITranscription factor II DCarrier ProteinsGene DeletionSmall nuclear RNATranscription Factors
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Physics of the nuclear pore complex: Theory, modeling and experiment

2021

Abstract The hallmark of eukaryotic cells is the nucleus that contains the genome, enclosed by a physical barrier known as the nuclear envelope (NE). On the one hand, this compartmentalization endows the eukaryotic cells with high regulatory complexity and flexibility. On the other hand, it poses a tremendous logistic and energetic problem of transporting millions of molecules per second across the nuclear envelope, to facilitate their biological function in all compartments of the cell. Therefore, eukaryotes have evolved a molecular “nanomachine” known as the Nuclear Pore Complex (NPC). Embedded in the nuclear envelope, NPCs control and regulate all the bi-directional transport between the…

Stochastic transportMolecular modelingGeneral Physics and AstronomyComputational biologyMolecular dynamics01 natural sciencesGenomeArticleDiffusionNanochannels0103 physical sciencesotorhinolaryngologic diseasesmedicineNuclear pore010306 general physicsPhysicsComputational modelIntrinsically disordered proteins010308 nuclear & particles physicsCompartmentalization (psychology)Nuclear pore complexCell nucleusCrowdingmedicine.anatomical_structureCytoplasmMultivalencyBiomimeticNucleusFunction (biology)Physics Reports
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dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8

2012

Toll-like receptor 3 (TLR3) is a pattern-recognition receptor known to initiate an innate immune response when stimulated by double-stranded RNA (dsRNA). Components of TLR3 signaling, including TIR domain-containing adapter inducing IFN-α (TRIF), have been demonstrated to contribute to dsRNA-induced cell death through caspase-8 and receptor interacting protein (RIP)1 in various human cancer cells. We provide here a detailed analysis of the caspase-8 activating machinery triggered in response to Poly(I:C) dsRNA. Engagement of TLR3 by dsRNA in both type I and type II lung cancer cells induces the formation of an atypical caspase-8-containing complex that is devoid of classical death receptors…

Ubiquitin-Protein LigasesvirusesApoptosischemical and pharmacologic phenomenaInhibitor of Apoptosis ProteinsCell Line TumorHumansFADDMolecular BiologyRNA Double-StrandedDeath domainCaspase 8Original PaperbiologyUbiquitinationRNA-Binding Proteinshemic and immune systemsMDA5Cell BiologyTNF Receptor-Associated Factor 2Fas receptorTRADDBaculoviral IAP Repeat-Containing 3 ProteinTNF Receptor-Associated Death Domain ProteinToll-Like Receptor 3Cell biologyNuclear Pore Complex ProteinsUbiquitin ligase complexDeath-inducing signaling complexTLR3biology.proteinSignal TransductionCell Death & Differentiation
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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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Import and impact : characterization of parvovirus-nucleus interactions

2016

tumakuljetusreseptoritviruksetkromatinisaatiomodification of nuclear architecturetumahuokosetcanine parvoviruspromotersnuclear transportDNApromoottoritinfektiotchromatinizationnuclear pore complextumaproteiinitparvovirukset
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