Search results for "Pore complex"

showing 10 items of 24 documents

Applications of Super Resolution Expansion Microscopy in Yeast

2021

Super-resolution microscopy includes multiple techniques in optical microscopy that enable sub-diffraction resolution fluorescence imaging of cellular structures. Expansion microscopy (EXM) is a method of physical expansion to obtain super-resolution images of a biological sample on conventional microscopy. We present images of yeast organelles, applying the combination of super-resolution and ExM techniques. When preparing pre-expanded samples, conventional methods lead to breakage of dividing yeast cells and difficulties in studying division-related proteins. Here, we describe an improved sample preparation technique that avoids such damage. ExM in combination with Airyscan and structured…

Fluorescence-lifetime imaging microscopyMaterials scienceMaterials Science (miscellaneous)BiophysicsGeneral Physics and Astronomyyeastlaw.invention03 medical and health sciences0302 clinical medicineOptical microscopelawnuclear pore complexMicroscopySample preparationPhysical and Theoretical ChemistryseptinMathematical Physics030304 developmental biology0303 health sciencesResolution (electron density)expansion super-resolutionImaging studySuperresolutionYeastlcsh:QC1-999tubulinBiological system030217 neurology & neurosurgerylcsh:PhysicsFrontiers in Physics
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Caspase-8 prevents sustained activation of NF-kappaB in monocytes undergoing macrophagic differentiation.

2006

Abstract Caspases have demonstrated several nonapoptotic functions including a role in the differentiation of specific cell types. Here, we show that caspase-8 is the upstream enzyme in the proteolytic caspase cascade whose activation is required for the differentiation of peripheral-blood monocytes into macrophages. On macrophage colony-stimulating factor (M-CSF) exposure, caspase-8 associates with the adaptor protein Fas-associated death domain (FADD), the serine/threonine kinase receptor-interacting protein 1 (RIP1) and the long isoform of FLICE-inhibitory protein FLIP. Overexpression of FADD accelerates the differentiation process that does not involve any death receptor. Active caspase…

Macrophage colony-stimulating factorCellular differentiationFas-Associated Death Domain ProteinImmunologyCaspase 8BiochemistryMonocytesArticle03 medical and health sciences0302 clinical medicineCell Line TumormedicineHumansFADDCaspase030304 developmental biologyDeath domain0303 health sciencesCaspase 8biologyMonocyteMacrophage Colony-Stimulating FactorMacrophagesNF-kappa BSignal transducing adaptor proteinRNA-Binding ProteinsCell DifferentiationCell BiologyHematologyMolecular biologyNuclear Pore Complex Proteinsmedicine.anatomical_structure030220 oncology & carcinogenesisbiology.proteinBlood
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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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Down-regulation of Glutathione and Bcl-2 Synthesis in Mouse B16 Melanoma Cells Avoids Their Survival during Interaction with the Vascular Endothelium

2003

B16 melanoma (B16M) cells with high GSH content show high metastatic activity. However, the molecular mechanisms linking GSH to metastatic cell survival are unclear. The possible relationship between GSH and the ability of Bcl-2 to prevent cell death was studied in B16M cells with high (F10) and low (F1) metastatic potential. Analysis of a Bcl-2 family of genes revealed that B16M-F10 cells, as compared with B16M-F1 cells, overexpressed preferentially Bcl-2 (approximately 5.7-fold). Hepatic sinusoidal endothelium-induced B16M-F10 cytotoxicity in vitro increased from approximately 19% (controls) to approximately 97% in GSH-depleted B16M-F10 cells treated with an antisense Bcl-2 oligodeoxynucl…

MaleProgrammed cell deathPore complexCell SurvivalMelanoma ExperimentalDown-RegulationOxidative phosphorylationBiologyBiochemistryOligodeoxyribonucleotides AntisenseMicechemistry.chemical_compoundDownregulation and upregulationCell Line TumorAnimalsButhionine SulfoximineMolecular BiologyBase SequenceTransition (genetics)Cell BiologyGlutathioneGlutathioneMolecular biologyGenes bcl-2Cell biologyMice Inbred C57BLOxidative StressCytosolchemistryEndothelium VascularEffluxCell DivisionJournal of Biological Chemistry
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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

Article

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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Evidence for a direct interaction of Rev protein with nuclear envelop mRNA-translocation system.

1991

The interaction of the Rev protein from human immunodeficiency virus type 1 (HIV-1) with the nucleocytoplasmic mRNA-transport system was investigated. In gel-shift assay, the recombinant Rev protein used in this study selectively bound to the Rev-responsive element (RRE) region of HIV-1 env-specific RNA. Nitrocellulose-filter-binding studies and Northern/Western-blotting experiments revealed an association constant of approximately 1 x 10(10) M-1. The Rev protein also strongly bound to isolated nuclear envelopes from H9 cells, containing the poly(A)-binding site (= mRNA carrier) and the nucleoside triphosphatase (= NTPase), which are thought to be involved in nuclear export of poly(A)-rich …

Pore complexPolyadenylationNuclear EnvelopevirusesBlotting WesternBiologyBiochemistryCell LineAdenosine TriphosphateAnimalsRNA MessengerNuclear porePhosphorylationNuclear export signalMessenger RNAVesicleRNABiological Transportrev Gene Products Human Immunodeficiency VirusBlotting NorthernNucleoside-TriphosphataseMolecular biologyPhosphoric Monoester HydrolasesRecombinant ProteinsCell biologyRatsBlotGene Products revHIV-1RNA ViralPoly AEuropean journal of biochemistry
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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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