Search results for "Nucleocytoplasmic Transport"

showing 10 items of 16 documents

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
researchProduct

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
researchProduct

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
researchProduct

Cargo transport through the nuclear pore complex at a glance.

2021

ABSTRACT Bidirectional transport of macromolecules across the nuclear envelope is a hallmark of eukaryotic cells, in which the genetic material is compartmentalized inside the nucleus. The nuclear pore complex (NPC) is the major gateway to the nucleus and it regulates nucleocytoplasmic transport, which is key to processes including transcriptional regulation and cell cycle control. Accordingly, components of the nuclear transport machinery are often found to be dysregulated or hijacked in diseases. In this Cell Science at a Glance article and accompanying poster, we provide an overview of our current understanding of cargo transport through the NPC, from the basic transport signals and mach…

Cell Nucleus0303 health sciencesBidirectional transportNuclear EnvelopeActive Transport Cell NucleusCell BiologyBiologyCell biologyNuclear Pore Complex Proteins03 medical and health sciences0302 clinical medicinemedicine.anatomical_structureEukaryotic CellsNucleocytoplasmic TransportCell cycle controlmedicineTranscriptional regulationNuclear PoreNuclear transportMultivalent bindingNuclear poreNucleus030217 neurology & neurosurgery030304 developmental biologyJournal of cell science
researchProduct

Kinetic models for nucleocytoplasmic transport of messenger RNA

1995

Abstract Much is known about the mechanism by which mRNAs cross the nuclear envelope (the translocation stage of nucleocytoplasmic transport), but far less is known about the preceding (intranuclear migration/release) and succeeding (cytoplasmic binding) stages. Therefore, existing information suffices for articulating detailed kinetic models of translocation, but not models for the overall mRNA transport process. In this paper, we show that simple kinetic models of translocation can (i) accommodate date about nucleocytoplasmic distributions of endogenous transcripts; (ii) predict the overall effects on these distributions of effectors such as insulin and epidermal growth factor; (iii) thro…

Cell NucleusStatistics and ProbabilityCytoplasmMessenger RNAModels GeneticGeneral Immunology and MicrobiologyMechanism (biology)EffectorApplied MathematicsChromosomal translocationGeneral MedicineBiologyTranslocation GeneticGeneral Biochemistry Genetics and Molecular BiologyCell biologyKineticsBiochemistryNucleocytoplasmic TransportEpidermal growth factorCytoplasmModeling and SimulationAnimalsMRNA transportRNA MessengerGeneral Agricultural and Biological SciencesJournal of Theoretical Biology
researchProduct

Heat shock protein 10 and signal transduction: a “capsula eburnea” of carcinogenesis?

2006

To date, little is known either about the physical interactions of heat shock protein 10 (Hsp10) with other proteins within the cell or its involvement in signal transduction pathways. Hsp10 has been considered mainly as a partner of Hsp60 in the Hsp60/10 protein folding machine. Only recently, Hsp10 was reported to interact with proteins involved in deoxyribonucleic acid checkpoint inactivation, termination of M-phase, messenger ribonucleic acid export, import of nuclear proteins, nucleocytoplasmic transport, and pheromone signaling pathways. At the same time, Hsp10 expression can be up-regulated in cancer cells, because it accumulates as the cell transformation progresses. Recent data sug…

Cell signalingColonCellular differentiationApoptosisChaperonin 60Cell BiologyBiologyCell cycleBiochemistryCell biologyFungal ProteinsBiochemistryHsp10 carcinogenesisNucleocytoplasmic TransportNeoplasmsHeat shock proteinColonic NeoplasmsChaperonin 10HumansHSP60MinireviewNuclear proteinSignal transductionSignal Transduction
researchProduct

The La antigen shuttles between the nucleus and the cytoplasm in CV-1 cells

1989

Recently we established a monoclonal antibody against the La-protein (Bachmann et al., Proc. Natl. Acad. Sci. USA, 83, 7770, 1986). The antibody gives a nuclear speckled type staining and, in addition, a perinuclear cytoplasmic staining on cultured cells in immunofluorescence microscopy. After inhibition of RNA synthesis the La-protein is transported into the cytoplasm. After prolonged inhibition it returns into the nucleus forming large growing speckles. The transport into the nucleus apparently depends on glycosylation.

CytoplasmGlycosylationmedicine.drug_classClinical BiochemistryFluorescent Antibody TechniqueMonoclonal antibodyAutoantigensCell Linechemistry.chemical_compoundmedicineAnimalsMolecular BiologyCell NucleusbiologyAutoantibodyAntibodies MonoclonalCell BiologyGeneral MedicineMolecular biologyStainingMolecular Weightmedicine.anatomical_structureRibonucleoproteinschemistryCytoplasmNucleocytoplasmic Transportbiology.proteinAntibodyProtein Processing Post-TranslationalNucleusTranscription FactorsMolecular and Cellular Biochemistry
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct