Search results for "Karyopherins"

showing 9 items of 19 documents

Centenarians maintain miRNA biogenesis pathway while it is impaired in octogenarians.

2016

Centenarians but not octogenarians up regulate the expression of miRNAs, as we previously reported. We have looked into miRNA biogenesis. We show that RNA POL II, DROSHA, EXPORTIN 5 and DICER, are up-regulated in centenarians compared with octogenarians. Furthermore, factors involved in the control of these miRNAs biogenesis genes are also up-regulated in centenarians. Therefore, the up-regulation of miRNA expression in centenarians can be explained in part because miRNA biogenesis pathway is depressed in octogenarians (ordinary aging) while it is maintained in centenarians (extraordinary aging).

Ribonuclease III0301 basic medicineAgingmedia_common.quotation_subjectRNA polymerase IIKaryopherinsBioinformaticsDEAD-box RNA Helicases03 medical and health sciencesmicroRNAHumansGeneDroshamedia_commonAged 80 and overGeneticsbiologyAge FactorsLongevityUp-RegulationMicroRNAs030104 developmental biologybiology.proteinRNA Polymerase IITranscriptomeMiRNA biogenesisBiogenesisDevelopmental BiologyDicer
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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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Yeast karyopherins Kap123 and Kap95 are related to the function of the cell integrity pathway

2009

The characterization of mutant strains in the gene encoding karyopherin Kap123 has revealed several morphogenetic defects. Inactivation of KAP123 caused alterations in the actin cytoskeleton, resulting in hyperpolarization and resistance to the actin polymerization inhibitor latrunculin B. In fact, the level of actin filaments is increased in kap123 mutant cells. In addition to the defect in actin cytoskeleton, the kap123 mutant cells showed a weakened cell wall, cell lysis and a growth defect in either the presence of sodium dodecyl sulfate or at high temperatures, which is alleviated by osmotic stabilizers. These defects in cell integrity and the actin cytoskeleton suggested a relationshi…

Saccharomyces cerevisiae ProteinsArp2/3 complexMADS Domain ProteinsSaccharomyces cerevisiaemacromolecular substancesApplied Microbiology and BiotechnologyMicrobiologyGene Knockout TechniquesCell WallNuclear proteinCytoskeletonCytoskeletonProtein kinase CActinMicroscopyMicrobial ViabilitybiologyActin remodelingGeneral Medicinebeta KaryopherinsActin cytoskeletonActinsCell biologybiology.proteinLatrunculinMitogen-Activated Protein KinasesFEMS Yeast Research
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Serum Response Factor-Mediated Gene Regulation in a Drosophila Visual Working Memory

2013

Summary Background Navigation through the environment requires a working memory for the chosen target and path integration facilitating an approach when the target becomes temporarily hidden. We have previously shown that this visual orientation memory resides in the ellipsoid body, which is part of the central complex in the Drosophila brain. Former analysis of  foraging and ignorant mutants have revealed that a hierarchical PKG and RSKII kinase signaling cascade in a subset of the ellipsoid-body ring neurons is required for this type of working memory in flies. Results Here we show that mutants in the ellipsoid body open  ( ebo ) gene, which encodes the actin-binding protein Exportin 6, e…

Serum Response FactorMutantKaryopherinsBiologyGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineOrientationCoactivatorSerum response factorNeuropilmedicineAnimalsDrosophila ProteinsTranscription factor030304 developmental biologyCell NucleusGeneticsRegulation of gene expression0303 health sciencesModels GeneticAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Working memoryMicrofilament ProteinsfungiLong-term potentiationActinsCell biologyDrosophila melanogasterMemory Short-Termmedicine.anatomical_structureGene Expression RegulationMutationVisual PerceptionGeneral Agricultural and Biological Sciences030217 neurology & neurosurgeryCurrent Biology
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Karyopherin Msn5 is involved in a novel mechanism controlling the cellular level of cell cycle regulators Cln2 and Swi5

2019

ABSTRACT The yeast β-karyopherin Msn5 controls the SBF cell-cycle transcription factor, responsible for the periodic expression of CLN2 cyclin gene at G1/S, and the nuclear export of Cln2 protein. Here we show that Msn5 regulates Cln2 by an additional mechanism. Inactivation of Msn5 causes a severe reduction in the cellular content of Cln2. This occurs by a post-transcriptional mechanism, since CLN2 mRNA level is not importantly affected in asynchronous cultures. Cln2 stability is not significantly altered in msn5 cells and inactivation of Msn5 causes a reduction in protein level even when Cln2 is stabilized. Therefore, the reduced amount of Cln2 in msn5 cells is mainly due not to a higher …

Swi50301 basic medicineSaccharomyces cerevisiae ProteinsS. cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeKaryopherinsCell cycleBiologyProtein degradationCyclin Gene03 medical and health sciences0302 clinical medicineCyclinsGene Expression Regulation FungalPolysomeProtein biosynthesisNuclear export signalMolecular BiologyTranscription factorCyclinMsn5 karyopherinCell BiologyCell cycleActinsCell biologyCln2 cyclin030104 developmental biologyMutagenesisPolyribosomesProtein Biosynthesis030220 oncology & carcinogenesisTranscription FactorsResearch PaperDevelopmental BiologyCell Cycle
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Regulation of cell cycle transcription factor Swi5 by karyopherin Msn5

2012

AbstractInactivation of S. cerevisiae β-karyopherin Msn5 causes hypersensitivity to the overexpression of mitotic cyclin Clb2 and aggravates growth defects of many mutant strains in mitotic exit, suggesting a connection between Msn5 and mitotic exit. We determined that Msn5 controlled subcellular localization of the mitotic exit transcription factor Swi5, since it was required for Swi5 nuclear export. Msn5 physically interacted with the N-terminal end of Swi5. Inactivation of Msn5 caused a severe reduction in cellular levels of Swi5 protein. This effect occurred by a post-transcriptional mechanism, since SWI5 mRNA levels were not affected. The reduced amount of Swi5 in msn5 mutant cells was…

Swi5Saccharomyces cerevisiae ProteinsGenes FungalActive Transport Cell NucleusMitosisCell Cycle ProteinsSaccharomyces cerevisiaeKaryopherinsProtein degradationBiologyNuclear export signalMolecular BiologyMitosisTranscription factorKaryopherinMsn5Cell Nucleuschemistry.chemical_classificationProtein StabilityCell CycleCell BiologyCell cycleβ-karyopherinMolecular biologyCell biologyProtein TransportchemistryMitotic exitMutationNuclear transportProtein BindingSubcellular FractionsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Yeast karyopherin Kap95 is required for cell cycle progression at Start

2010

Abstract Background The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. Results When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel r…

Transcriptional ActivationSaccharomyces cerevisiae ProteinsNuclear Localization SignalsActive Transport Cell NucleusSaccharomyces cerevisiaeImportinBiologylcsh:QH573-671Transcription factorCells CulturedKaryopherinCell Nucleuschemistry.chemical_classificationlcsh:CytologyCell CycleCell BiologyCell cyclebeta KaryopherinsSubcellular localizationCell biologyDNA-Binding ProteinschemistryCytoplasmMutationTranscription Initiation SiteNuclear transportNuclear localization sequenceProtein BindingTranscription FactorsResearch ArticleBMC Cell Biology
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Human inducible nitric oxide synthase (iNOS) expression depends on chromosome region maintenance 1 (CRM1)- and eukaryotic translation initiation fact…

2012

Human inducible nitric oxide synthase (iNOS) is regulated on the expressional level mostly by post-transcriptional mechanisms modulating the mRNA stability. Another important step in the control of eukaryotic gene expression is the nucleocytoplasmic mRNA transport. Most cellular mRNAs are exported via the TAP/Nxt complex of proteins. However, some mRNAs are transported by a different mechanism involving the nuclear export receptor CRM1. Treatment of DLD-1 cells with the CRM1 inhibitor leptomycin B (LMB) or anti-CRM1 siRNAs reduced cytokine-induced iNOS expression. We could demonstrate that the iNOS mRNA is exported from the nucleus in a CRM1-dependent manner. Since CRM1 itself does not poss…

Untranslated regionCancer ResearchPhysiologyClinical BiochemistryActive Transport Cell NucleusNitric Oxide Synthase Type IIReceptors Cytoplasmic and NuclearKaryopherinsBiologyenvironment and public healthBiochemistryRNA TransportEukaryotic translationCell Line TumorRibavirinGene expressionP-bodiesHumansMRNA transportRNA MessengerLuciferasesNuclear export signalAnalysis of VarianceMessenger RNAfungiEIF4EMolecular biologyEukaryotic Initiation Factor-4Elipids (amino acids peptides and proteins)Nitric Oxide
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Cytoplasmic Parvovirus Capsids Recruit Importin Beta for Nuclear Delivery

2019

Parvoviruses are an important platform for gene and cancer therapy. Their cell entry and the following steps, including nuclear import, are inefficient, limiting their use in therapeutic applications. Two models exist on parvoviral nuclear entry: the classical import of the viral capsid using nuclear transport receptors of the importin (karyopherin) family or the direct attachment of the capsid to the nuclear pore complex leading to the local disintegration of the nuclear envelope. Here, by laser scanning confocal microscopy and in situ proximity ligation analyses combined with coimmunoprecipitation, we show that infection requires importin β-mediated access to the nuclear pore complex and …

alpha KaryopherinsCytoplasmNuclear EnvelopevirusesImmunologyActive Transport Cell NucleusImportinKaryopherinsBiologyVirus ReplicationMicrobiologyCell LineParvoviridae InfectionsParvovirus03 medical and health sciencesCapsidCytosolViral entryVirologyAnimalsNuclear pore030304 developmental biologyKaryopherinCell Nucleuschemistry.chemical_classification0303 health sciencesNucleoplasm030302 biochemistry & molecular biologyVirus Internalizationbeta KaryopherinsVirus-Cell InteractionsCell biologychemistryCytoplasmInsect ScienceNuclear PoreCapsid ProteinsNucleoporinNuclear transportJournal of Virology
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