Search results for "nuclear localization sequence"

showing 10 items of 27 documents

Survivin’s Dual Role: An Export’s View

2007

Survivin is proposed to function as a mitotic regulator and an apoptosis inhibitor during development and pathogenesis. As such, survivin has aroused keen interest in disparate areas of basic and translational research. Survivin acts as a subunit of the chromosomal passenger complex (CPC), composed of the mitotic kinase Aurora-B, Borealin and INCENP, and is essential for proper chromosome segregation and cytokinesis. Our recent findings indicate that the nuclear export receptor Crm1 is critically involved in tethering the CPC to the centromere by interacting with a leucine-rich nuclear export signal (NES), evolutionary conserved in all mammalian survivin proteins. In addition, the survivin/…

Cell NucleusApoptosis InhibitorINCENPSurvivinActive Transport Cell NucleusCell BiologyCell cycleBiologyInhibitor of Apoptosis ProteinsNeoplasm ProteinsCell biologySurvivinAnimalsHumansNuclear export signalMicrotubule-Associated ProteinsneoplasmsMolecular BiologyMitosisCytokinesisNuclear localization sequenceDevelopmental BiologyCell Cycle
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Differential subcellular expression of P525LFUS as a putative biomarker for ALS phenoconversion

2020

P525LFused-in-Sarcoma ( FUS ) mutation is associated with a specific amyotrophic lateral sclerosis (ALS) phenotype characterized by a juvenile-onset and a severe course.1 This harmful point mutation is located in the nuclear localization signal (NLS) domain at the protein C-terminal.2 Although wild-type FUS protein is expressed almost exclusively in the nucleus, the P525L FUS mutation leads to a protein mislocalization into the cytoplasm3,4 because of its loss of capacity to bind its transporter karyopherin-2 and to be transferred back to the nucleus.3

0301 basic medicineMutationPoint mutationTransporterALS FUS fibroblastsBiologymedicine.disease_causemedicine.diseasePhenotypeCell biology03 medical and health sciences030104 developmental biology0302 clinical medicinemedicine.anatomical_structuremedicineNLSSettore MED/26 - NeurologiaNeurology (clinical)Amyotrophic lateral sclerosisNucleus030217 neurology & neurosurgeryGenetics (clinical)Nuclear localization sequence
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Hypoxia-Induced miR-675-5p Supports β-Catenin Nuclear Localization by Regulating GSK3-β  Activity in Colorectal Cancer Cell Lines

2020

The reduction of oxygen partial pressure in growing tumors triggers numerous survival strategies driven by the transcription factor complex HIF1 (Hypoxia Inducible Factor-1). Recent evidence revealed that HIF1 promotes rapid and effective phenotypic changes through the induction of non-coding RNAs, whose contribution has not yet been fully described. Here we investigated the role of the hypoxia-induced, long non-coding RNA H19 (lncH19) and its intragenic miRNA (miR-675-5p) into HIF1-Wnt crosstalk. During hypoxic stimulation, colorectal cancer cell lines up-regulated the levels of both the lncH19 and its intragenic miR-675-5p. Loss of expression experiments revealed that miR-675-5p inhibitio…

0301 basic medicineTranscription factor complexKaplan-Meier Estimatelcsh:Chemistry0302 clinical medicineGSK-3poxiahylcsh:QH301-705.5long non-coding H19Spectroscopybeta CateninKinaseChemistryGeneral MedicineCell HypoxiaComputer Science ApplicationsCell biologyGene Expression Regulation Neoplastic030220 oncology & carcinogenesisColorectal NeoplasmsProtein BindingActive Transport Cell Nucleuscolorectal cancermiR-675TransfectionCatalysisArticleInorganic Chemistry03 medical and health sciencesCell Line TumormicroRNAGene silencingHumansPhysical and Theoretical ChemistryMolecular BiologyGlycogen Synthase Kinase 3 betahypoxiaOrganic ChemistryRNAComputational Biologyβ-cateninHCT116 CellsMicroRNAs030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Microscopy FluorescenceCateninMutationNuclear localization sequenceInternational Journal of Molecular Sciences
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Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

2003

Abstract We have recently shown that the minor capsid protein L2 of human papillomavirus type 33 (HPV33) recruits the transcriptional repressor Daxx into nuclear domains (ND) 10 and causes the loss of the transcriptional activator Sp100 from these subnuclear structures (Florin et al., 2002b) . In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed. Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (S…

ImmunoprecipitationRecombinant Fusion ProteinsGreen Fluorescent ProteinsNuclear Localization SignalsActive Transport Cell NucleusFluorescent Antibody TechniqueBiologyImmunofluorescenceAutoantigensGreen fluorescent proteinDeath-associated protein 6DaxxVirologyTumor Cells CulturedmedicineSp100HumansNLSPapillomaviridaeAdaptor Proteins Signal TransducingCell Nucleusmedicine.diagnostic_testIntracellular Signaling Peptides and ProteinsND10Nuclear ProteinsAntigens NuclearL2Oncogene Proteins ViralPapillomavirusbiochemical phenomena metabolism and nutritionMolecular biologyDeletion MutagenesisLuminescent ProteinsCapsidMutagenesisCapsid ProteinsCarrier ProteinsCo-Repressor ProteinsGene DeletionNuclear localization sequenceMolecular ChaperonesVirology
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Attenuation of NF-κB Signaling Response to UVB Light during Cellular Senescence

1999

The ability of cells to adapt to environmental stresses undergoes a progressive reduction during aging. NF-kappaB-mediated signaling is a major defensive system against various environmental challenges. The aim of this study was to find out whether replicative senescence affects the response of the NF-kappaB signaling pathway to UVB light in human WI-38 and IMR-90 fibroblasts. The exposure of early passage fibroblasts to UVB light inhibited the proliferation and induced a flat phenotype similar to that observed in replicatively senescent fibroblasts not exposed to UVB light. The UVB radiation dose used (153 mJ/cm2) did not induce apoptosis in either early or late passage WI-38 fibroblasts. …

SenescenceP50Ultraviolet RaysLactams MacrocyclicBiologyCell LineBenzoquinonesHumansEnzyme InhibitorsProtein Kinase InhibitorsCellular SenescenceCell Line TransformedNF-kappa BQuinonesCell BiologyFibroblastsTyrphostinsMolecular biologyIκBαRifabutinApoptosisPhosphorylationTumor necrosis factor alphaSignal transductionNuclear localization sequenceSignal TransductionExperimental Cell Research
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Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells

2004

AbstractA mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protei…

Parvovirus CanineRecombinant Fusion Proteinsanimal diseasesvirusesGreen Fluorescent ProteinsBiophysicsMammalian expressionBiochemistryCell LineGreen fluorescent proteinTransduction (genetics)DogsTransduction GeneticStructural BiologyGeneticsAnimalsBaculovirusCanine parvovirusMolecular BiologyCell NucleusEnhanced green fluorescent proteinbiologyParvovirusCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyCell biologyCapsidCytoplasmCell cultureCatsCapsid ProteinsBaculoviridaeNuclear localization sequenceFEBS Letters
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RNA-controlled nucleocytoplasmic shuttling of mRNA decay factors regulates mRNA synthesis and initiates a novel mRNA decay pathway

2021

AbstractmRNA level is controlled by factors that mediate both mRNA synthesis and decay, including the exonuclease Xrn1 - a major mRNA synthesis and decay factor. Here we show that nucleocytoplasmic shuttling of Xrn1 and of some of its associated mRNA decay factors plays a key role in determining both mRNA synthesis and decay. Shuttling is regulated by RNA-controlled binding of the karyopherin Kap120 to two nuclear localization sequences (NLSs) in Xrn1. The decaying RNA binds and masks NLS1, establishing a link between mRNA decay and Xrn1 shuttling. Mutations in the two NLSs, which prevent Xrn1 import, compromise transcription and, unexpectedly, also the cytoplasmic decay of ∼50% of the cell…

chemistry.chemical_classificationExonuclease0303 health sciencesbiology030302 biochemistry & molecular biologyMRNA DecayRNACell biology03 medical and health sciencesmedicine.anatomical_structurechemistryCytoplasmTranscription (biology)medicinebiology.proteinNucleusNuclear localization sequence030304 developmental biologyKaryopherin
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Identification of a classic nuclear localization signal at the N terminus that regulates the subcellular localization of Rbfox2 isoforms during diffe…

2016

Nuclear localization of the alternative splicing factor Rbfox2 is achieved by a C-terminal nuclear localization signal (NLS) which can be excluded from some Rbfox2 isoforms by alternative splicing. While this predicts nuclear and cytoplasmic localization, Rbfox2 is exclusively nuclear in some cell types. Here, we identify a second NLS in the N terminus of Rbfox2 isoform 1A that is not included in Rbfox2 isoform 1F. Rbfox2 1A isoforms lacking the C-terminal NLS are nuclear, whereas equivalent 1F isoforms are cytoplasmic. A shift in Rbfox2 expression toward cytoplasmic 1F isoforms occurs during epithelial to mesenchymal transition (EMT) and could be important in regulating the activity and fu…

0301 basic medicineGene isoformCytoplasmEpithelial-Mesenchymal TransitionNuclear Localization SignalsBiophysicsBiochemistryCell LineTransforming Growth Factor beta103 medical and health sciencesMiceMammary Glands AnimalProtein DomainsStructural BiologyCell Line TumorGeneticsNLSAnimalsProtein IsoformsAmino Acid SequenceMolecular BiologyCell NucleusChemistryAlternative splicingCell DifferentiationEpithelial CellsMouse Embryonic Stem CellsCell BiologySubcellular localizationMolecular biologyCell biologyAlternative Splicing030104 developmental biologyP19 cellCytoplasmRNA splicingRNA Splicing FactorsSequence AlignmentNuclear localization sequenceSignal TransductionFEBS letters
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Zfp819, a novel KRAB-zinc finger protein, interacts with KAP1 and functions in genomic integrity maintenance of mouse embryonic stem cells

2013

AbstractPluripotency is maintained by both known and unknown transcriptional regulatory networks. In the present study, we have identified Zfp819, a KRAB-zinc finger protein, as a novel pluripotency-related factor and characterized its role in pluripotent stem cells. We show that Zfp819 is expressed highly in various types of pluripotent stem cells but not in their differentiated counterparts. We identified the presence of non-canonical nuclear localization signals in particular zinc finger motifs and identified them as responsible for the nuclear localization of Zfp819. Analysis of the Zfp819 promoter region revealed the presence of a transcriptionally active chromatin signature. Moreover,…

Homeobox protein NANOGMolecular Sequence DataEndogenous retrovirusBiologyTripartite Motif-Containing Protein 28Cell LineHistones03 medical and health sciencesMice0302 clinical medicineSOX2AnimalsAmino Acid SequenceRNA Small InterferingInduced pluripotent stem cellPromoter Regions GeneticEmbryonic Stem Cells030304 developmental biologyTranscriptionally active chromatinZinc fingerMedicine(all)Cell NucleusHomeodomain Proteins0303 health sciencesSOXB1 Transcription FactorsNuclear ProteinsCell DifferentiationGeneral MedicineCell BiologyNanog Homeobox ProteinMolecular biologyEmbryonic stem cellUp-RegulationDNA-Binding ProteinsRepressor Proteins030220 oncology & carcinogenesisCarrier ProteinsOctamer Transcription Factor-3Nuclear localization sequenceDevelopmental BiologyDNA DamageProtein BindingStem Cell Research
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Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptio…

2002

The subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes, is modulated by carbon source availability. In cells growing in glucose, Msn2 is located mainly in the cytosol, whereas in carbon source-starved cells, Msn2 is located largely inside the nucleus. However, in cells lacking Reg1 (the regulatory subunit of the Reg1/Glc7 protein phosphatase complex), the regulation of subcellular distribution is absent, Msn2 being constitutively present in the cytosol. The localization defect in these mutants is specific for carbon starvation stress, and it is because of the presence of an abnormally active Snf1 protein kinase that inhibits the n…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeMitogen-activated protein kinase kinaseBiologyProtein Serine-Threonine KinasesBiochemistryASK1Molecular BiologyDNA PrimersSirolimusMAP kinase kinase kinaseBase SequenceKinaseCell BiologySubcellular localizationCarbonCell biologyCulture MediaDNA-Binding ProteinsCytosolBiochemistryTrans-ActivatorsCyclin-dependent kinase 9Nuclear localization sequenceSubcellular FractionsTranscription FactorsThe Journal of biological chemistry
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