Search results for "nucleocytoplasmic transport"

showing 10 items of 16 documents

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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Protein traffic is an intracellular target in alcohol toxicity

2011

Eukaryotic cells comprise a set of organelles, surrounded by membranes with a unique composition, which is maintained by a complex synthesis and transport system. Cells also synthesize the proteins destined for secretion. Together, these processes are known as the secretory pathway or exocytosis. In addition, many molecules can be internalized by cells through a process called endocytosis. Chronic and acute alcohol (ethanol) exposure alters the secretion of different essential products, such as hormones, neurotransmitters and others in a variety of cells, including central nervous system cells. This effect could be due to a range of mechanisms, including alcohol-induced alterations in the d…

BiologiaAntropologia físicaCellneuronsPharmaceutical ScienceReviewBiologyEndocytosisBioinformaticsExocytosisDrug DiscoverymedicineSecretionCytoskeletonSecretory pathwaynucleocytoplasmic transportastrocytesCell biologyVesicular transport proteinmedicine.anatomical_structurePsicobiologiaMolecular Medicineethanolintracellular trafficIntracellular
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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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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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Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET

2018

Abstract Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex. They are highly dynamic under physiological conditions and studying their interaction with nuclear transport receptors (NTRs) is key to understanding the molecular mechanism of nucleocytoplasmic transport. Distinct conformational features of FG-Nups interacting with diverse NTRs can be detected by multiparameter single-molecule fluorescence energy transfer (smFRET), which is a powerful technique for studying the dynamics and interactions of biomolecules in solution. Here we provide a detailed protocol utilizing smFRET to reveal dif…

0301 basic medicineModels MolecularGlycosylationProtein ConformationPhenylalanineGlycineIntrinsically disordered proteinsArticle03 medical and health scienceschemistry.chemical_compoundFluorescence Resonance Energy TransferAnimalsHumansNuclear porechemistry.chemical_classificationBiomoleculeSingle-molecule FRETEquipment DesignIntrinsically Disordered ProteinsNuclear Pore Complex Proteins030104 developmental biologychemistryNucleocytoplasmic TransportBiophysicsNucleoporinNuclear transportProtein BindingIntrinsically Disordered Proteins
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Molecular determinants of large cargo transport into the nucleus

2020

Nucleocytoplasmic transport is tightly regulated by the nuclear pore complex (NPC). Among the thousands of molecules that cross the NPC, even very large (>15 nm) cargoes such as pathogens, mRNAs and pre-ribosomes can pass the NPC intact. For these cargoes, there is little quantitative understanding of the requirements for their nuclear import, especially the role of multivalent binding to transport receptors via nuclear localisation sequences (NLSs) and the effect of size on import efficiency. Here, we assayed nuclear import kinetics of 30 large cargo models based on four capsid-like particles in the size range of 17–36 nm, with tuneable numbers of up to 240 NLSs. We show that the requireme…

QH301-705.5ScienceStructural Biology and Molecular Biophysicspermeabilized cellsimport kineticsNuclear Localization SignalsBiophysicslarge cargoActive Transport Cell NucleusNLSnuclear transportGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicinemedicinecapsidNLSHumansNuclear poreBiology (General)030304 developmental biologyCell Nucleus0303 health sciencesGeneral Immunology and MicrobiologyChemistryGeneral NeuroscienceMolecular biophysicsQRE. coliGeneral MedicineCell Biologymedicine.anatomical_structureStructural biologyNucleocytoplasmic TransportBiophysicsNuclear PoreMedicineNuclear transportCarrier ProteinsFlux (metabolism)Nucleus030217 neurology & neurosurgeryResearch ArticleHumaneLife
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Nucleocytoplasmic transport of the RNA-binding protein CELF2 regulates neural stem cell fates.

2020

The development of the cerebral cortex requires balanced expansion and differentiation of neural stem/progenitor cells (NPCs), which rely on precise regulation of gene expression. Because NPCs often exhibit transcriptional priming of cell-fate-determination genes, the ultimate output of these genes for fate decisions must be carefully controlled in a timely fashion at the post-transcriptional level, but how that is achieved is poorly understood. Here, we report that de novo missense variants in an RNA-binding protein CELF2 cause human cortical malformations and perturb NPC fate decisions in mice by disrupting CELF2 nucleocytoplasmic transport. In self-renewing NPCs, CELF2 resides in the cyt…

0301 basic medicineRegulation of gene expressionNeurogenesisRNA-Binding ProteinsTranslation (biology)RNA-binding proteinCell DifferentiationNerve Tissue ProteinsBiologyCell fate determinationGeneral Biochemistry Genetics and Molecular BiologyNeural stem cellCell biology03 medical and health sciences030104 developmental biology0302 clinical medicineNeural Stem CellsNucleocytoplasmic TransportCELF ProteinsHumansProgenitor cell030217 neurology & neurosurgeryCell reports
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Transport of mRNA from Nucleus to Cytoplasm

1987

Publisher Summary Transport of mRNP (messenger ribonucleoprotein) from nucleus to cytoplasm plays an important role in gene expression in eukaryotic cells. This chapter focuses on energy-(ATP)-dependent mRNP transport. Nucleocytoplasmic transport of ribosomal RNA can also be induced by ATP, but also occurs by varying [Ca 2+ ]:[Mg 2+ ]. Release of ribosomal RNPs seems to be accompanied by an expansion of the nucleus. Nucleocytoplasmic transport of mRNA seems to be also distinct from the export of tRNA or the exchange of snRNPs and proteins across the nuclear envelope. Nucleocytoplasmic transport of tRNA seems to involve a facilitated diffusion mechanism, showing saturability and sequence spe…

Messenger RNPCell nucleusmedicine.anatomical_structureBiochemistryCytoplasmNucleocytoplasmic TransportmedicinesnRNPNuclear poreBiologyNuclear export signalNucleusCell biology
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Translocation Biosensors – Cellular System Integrators to Dissect CRM1-Dependent Nuclear Export by Chemicogenomics

2009

Fluorescent protein biosensors are powerful cellular systems biology tools for dissecting the complexity of cellular processes with high spatial and temporal resolution. As regulated nucleo-cytoplasmic transport is crucial for the modulation of numerous (patho)physiological cellular responses, a detailed understanding of its molecular mechanism would open up novel options for a rational manipulation of the cell. In contrast to genetic approaches, we here established and employed high-content cellular translocation biosensors applicable for dissecting nuclear export by chemicogenomics. A431 cell lines, stably expressing a translocation biosensor composed of glutathione S-transferase, GFP and…

Systems biologyChemical biologyNanotechnologychemical biologyComputational biologyBiologylcsh:Chemical technologyBiochemistryArticleAnalytical ChemistryGreen fluorescent proteinFlow cytometrychemical biology; cancer; Exportin 1/CRM1; HIV-1 Rev; import; LMB; nucleocytoplasmic transport; nucleoporinimportmedicinecancerlcsh:TP1-1185Electrical and Electronic EngineeringNuclear export signalLMBInstrumentationExportin 1/CRM1HIV-1 Revnucleocytoplasmic transportmedicine.diagnostic_testnucleoporinAtomic and Molecular Physics and OpticsChemical spacecancer ; HIV-1 Rev ; import ; nucleocytoplasmic transport ; LMB ; chemical biology ; Exportin 1/CRM1 ; nucleoporinNucleoporinNuclear transportBiologieSensors
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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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