Search results for "nuclear pore complex"

showing 10 items of 20 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

Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

2018

Summary Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lowe…

0301 basic medicineModels MolecularGlycosylationglycosylationProtein ConformationPhenylalanineGlycineSequence (biology)Intrinsically disordered proteinsnuclear transport receptorssingle-molecule FRETGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEscherichia coliFluorescence Resonance Energy TransferHumansNuclear poreReceptorlcsh:QH301-705.5Single-molecule FRETmolecular dynamics simulationsbinding mechanismintrinsically disordered proteinFG-Nup3. Good healthNuclear Pore Complex Proteins030104 developmental biologychemistrylcsh:Biology (General)BiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryProtein BindingCell Reports
researchProduct

Protoparvovirus Knocking at the Nuclear Door

2017

Protoparvoviruses target the nucleus due to their dependence on the cellular reproduction machinery during the replication and expression of their single-stranded DNA genome. In recent years, our understanding of the multistep process of the capsid nuclear import has improved, and led to the discovery of unique viral nuclear entry strategies. Preceded by endosomal transport, endosomal escape and microtubule-mediated movement to the vicinity of the nuclear envelope, the protoparvoviruses interact with the nuclear pore complexes. The capsids are transported actively across the nuclear pore complexes using nuclear import receptors. The nuclear import is sometimes accompanied by structural chan…

0301 basic medicinevirusesimportinsActive Transport Cell Nucleuslcsh:QR1-502Genome ViralReviewImportinKaryopherinsBiologyVirus Replicationlcsh:MicrobiologyParvovirusMice03 medical and health sciencesCapsidVirologynuclear pore complexmedicineAnimalsHumansInner membraneNuclear poreprotoparvovirusCell Nucleusnuclear localization sequence030102 biochemistry & molecular biologyta1182nuclear envelopeVirus InternalizationVirologynuclear importCell biologyCell nucleusnuclear envelope break down030104 developmental biologyInfectious Diseasesmedicine.anatomical_structureintracellular dynamicsEndosomal transportNuclear PoreentryCapsid ProteinsNucleoporinNuclear transportNuclear localization sequenceViruses
researchProduct

Analysis of translocations that involve theNUP98 gene in patients with 11p15 chromosomal rearrangements

2004

The NUP98 gene has been reported to be fused with at least 15 partner genes in leukemias with 11p15 translocations. We report the results of screening of cases with cytogenetically documented rearrangements of 11p15 and the subsequent identification of involvement of NUP98 and its partner genes. We identified 49 samples from 46 hematology patients with 11p15 (including a few with 11p14) abnormalities, and using fluorescence in situ hybridization (FISH), we found that NUP98 was disrupted in 7 cases. With the use of gene-specific FISH probes, in 6 cases, we identified the partner genes, which were PRRX1 (PMX1; in 2 cases), HOXD13, RAP1GDS1, HOXC13, and TOP1. In the 3 cases for which RNA was a…

AdultMaleCancer Researchmedicine.medical_specialtyAdolescentMolecular Sequence DataChromosomal translocationBiologyTranslocation GeneticComplementary DNAInternal medicineGeneticsmedicineGuanine Nucleotide Exchange FactorsHumansGenetic Predisposition to DiseaseGeneIn Situ Hybridization FluorescenceHomeodomain ProteinsGeneticsNUP98 GeneLeukemiaHematologyBase Sequencemedicine.diagnostic_testChromosomes Human Pair 11BreakpointInfantMolecular biologyNuclear Pore Complex ProteinsDNA Topoisomerases Type IHOXD13Child PreschoolTranscription FactorsFluorescence in situ hybridizationGenes, Chromosomes and Cancer
researchProduct

Midregion PTHrP regulates Rip1 and caspase expression in MDA-MB231 breast cancer cells.

2007

It was previously reported that the midregion PTHrP domain (38-94)-amide restrains growth and invasion "in vitro", causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231 whose tumorigenesis was also attenuated "in vivo". In addition, we have demonstrated that midregion PTHrP is imported in the nucleoplasm of cultured MDA-MB231 cells, and that "in vitro" it can bind chromatin of metaphase spread preparations and also an isolated 20-mer oligonucleotide, thereby appearing endowed with a putative transcription factor-like DNA-binding ability. Here, we examined whether PTHrP (38-94)-amide was able to modulate the expression of genes e…

Cancer ResearchProgrammed cell deathbcl-X ProteinApoptosisBreast NeoplasmsPTHrP Rip1 caspase breast cancer cellsmedicine.disease_causeTransfectionCell MovementCell Line TumorGene expressionmedicineTranscriptional regulationHumansNeoplasm InvasivenessSettore BIO/06 - Anatomia Comparata E Citologiaskin and connective tissue diseasesCaspaseCell ProliferationNucleoplasmbiologyJNK Mitogen-Activated Protein KinasesParathyroid Hormone-Related ProteinRNA-Binding ProteinsOligonucleotides AntisenseMolecular biologyPeptide FragmentsChromatinCell biologyNuclear Pore Complex ProteinsSettore BIO/12 - Biochimica Clinica E Biologia Molecolare ClinicaOncologyApoptosisCaspasesbiology.proteinFemalebcl-Associated Death ProteinCarcinogenesisSignal TransductionBreast cancer research and treatment
researchProduct

Parthenolide generates reactive oxygen species and autophagy in MDA-MB231 cells. A soluble parthenolide analogue inhibits tumour growth and metastasi…

2013

Triple-negative breast cancers (TNBCs) are clinically aggressive forms associated with a poor prognosis. We evaluated the cytotoxic effect exerted on triple-negative MDA-MB231 breast cancer cells both by parthenolide and its soluble analogue dimethylamino parthenolide (DMAPT) and explored the underlying molecular mechanism. The drugs induced a dose- and time-dependent decrement in cell viability, which was not prevented by the caspase inhibitor z-VAD-fmk. In particular in the first hours of treatment (1–3 h), parthenolide and DMAPT strongly stimulated reactive oxygen species (ROS) generation. The drugs induced production of superoxide anion by activating NADPH oxidase. ROS generation caused…

Cancer ResearchautophagyCell SurvivalparthenolideFas-Associated Death Domain ProteinImmunologyCASP8 and FADD-Like Apoptosis Regulating ProteinBreast Neoplasmsparthenolide; ROS; NOX; autophagy; breast cancer xenograft.MiceCellular and Molecular Neurosciencechemistry.chemical_compoundDownregulation and upregulationCell Line TumorSettore BIO/10 - BiochimicaAnimalsHumansParthenolidePropidium iodidebreast cancer xenograftMembrane Potential Mitochondrialchemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologybreast cancer xenograft.SuperoxideNF-kappa BRNA-Binding ProteinsROSCell BiologyNOXXenograft Model Antitumor AssaysMolecular biologyNuclear Pore Complex ProteinsVascular endothelial growth factorchemistryCell cultureCancer researchbiology.proteinCalciumFemaleOriginal ArticleReactive Oxygen SpeciesSesquiterpenes
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

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

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
researchProduct

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
researchProduct