Search results for " Cell Nucleus"

showing 10 items of 62 documents

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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Physical and Genetic Interactions Link the Yeast Protein Zds1p with mRNA Nuclear Export

2005

Eukaryotic gene expression requires the export of mRNA from the nucleus to the cytoplasm. The DEAD box protein Dbp5p is an essential export factor conserved from yeast to man. A fraction of Dbp5p forms a complex with nucleoporins of the cytoplasmic filaments of the nuclear pore complex. Gfd1p was identified originally as a multicopy suppressor of the rat8-2 ts allele of DBP5. Here we reported that Dbp5p and Gfd1p interact with Zds1p, a protein previously identified as a multicopy suppressor in several yeast genetic screens. By using the two-hybrid system, we showed that Zds1p interacts in vivo with both Gfd1p and Dbp5p. In vitro binding experiments revealed that Gfd1p and Dbp5p bind directl…

Saccharomyces cerevisiae ProteinsMolecular Sequence DataMutantActive Transport Cell NucleusSaccharomyces cerevisiaeBiologyBiochemistryCytosolGene expressionmedicineRNA MessengerNuclear poreNuclear export signalMolecular BiologyAdaptor Proteins Signal TransducingDNA PrimersGeneticsMessenger RNABase SequenceNuclear cap-binding protein complexRNA FungalCell BiologyCell biologyCell nucleusmedicine.anatomical_structureNucleoporinGenome FungalJournal of Biological Chemistry
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The mitotic kinase Aurora-A promotes distant metastases by inducing epithelial-to-mesenchymal transition in ERα+ breast cancer cells

2013

In this study, we demonstrate that constitutive activation of Raf-1 oncogenic signaling induces stabilization and accumulation of Aurora-A mitotic kinase that ultimately drives the transition from an epithelial to a highly invasive mesenchymal phenotype in estrogen receptor α-positive (ERα(+)) breast cancer cells. The transition from an epithelial- to a mesenchymal-like phenotype was characterized by reduced expression of ERα, HER-2/Neu overexpression and loss of CD24 surface receptor (CD24(-/low)). Importantly, expression of key epithelial-to-mesenchymal transition (EMT) markers and upregulation of the stemness gene SOX2 was linked to acquisition of stem cell-like properties such as the ab…

Smad5 ProteinCancer ResearchEpithelial-Mesenchymal TransitionMAP Kinase Signaling SystemReceptor ErbB-2Active Transport Cell NucleusEstrogen receptorMice NudeBreast NeoplasmsBiologyArticleMicebreast cancerSOX2Cell MovementCell Line TumorGeneticsAnimalsHumansEpithelial–mesenchymal transitionKinase activityNeoplasm MetastasisPhosphorylationRNA Small InterferingMolecular BiologyAurora Kinase Ametastases mitosisSOXB1 Transcription FactorsEstrogen Receptor alphaCD24 AntigenXenograft Model Antitumor AssaysstemneGene Expression Regulation NeoplasticProto-Oncogene Proteins c-rafSettore BIO/18 - GeneticaTumor progressionembryonic structuresCancer researchMCF-7 CellsNeoplastic Stem CellsProto-Oncogene Proteins c-rafFemaleRNA InterferenceSignal transductionEstrogen receptor alphaNeoplasm Transplantation
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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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Paclitaxel and beta-lapachone synergistically induce apoptosis in human retinoblastoma Y79 cells by downregulating the levels of phospho-Akt.

2009

Paclitaxel (PTX) and beta-lapachone (LPC) are naturally occurring compounds that have shown a large spectrum of anticancer activity. In this article we show for the first time that PTX/LPC combination induces potent synergistic apoptotic effects in human retinoblastoma Y79 cells. Combination of suboptimal doses of PTX (0.3 nM) and LPC (1.5 microM) caused biochemical and morphological signs of apoptosis at 48 h of treatment. These effects were accompanied by potent lowering in inhibitor of apoptosis proteins and by activation of Bid and caspases 3 and 6 with lamin B and PARP breakdown. PTX/LPC combination acted by favoring p53 stabilization through a lowering in p-Akt levels and in ps166-MDM…

Time FactorsPhysiologyClinical BiochemistryApoptosisInhibitor of Apoptosis ProteinsWortmanninchemistry.chemical_compoundSettore BIO/10 - BiochimicaAntineoplastic Combined Chemotherapy ProtocolsPhosphorylationCaspasebiologyCaspase 6Lamin Type BCaspase 3Protein StabilityRetinoblastomaDrug SynergismProto-Oncogene Proteins c-mdm2TransfectionBiochemistrylipids (amino acids peptides and proteins)Poly(ADP-ribose) PolymerasesWortmanninBH3 Interacting Domain Death Agonist Proteinretinoblastoma survival factors apoptosisPaclitaxelCell SurvivalPoly ADP ribose polymeraseActive Transport Cell NucleusDown-RegulationInhibitor of apoptosisTransfectionCell Line TumorHumansProtein kinase BProtein Kinase InhibitorsCell NucleusDose-Response Relationship DrugCell BiologyAntineoplastic Agents PhytogenicAndrostadieneschemistryCell cultureApoptosisbiology.proteinCancer researchTumor Suppressor Protein p53Proto-Oncogene Proteins c-aktNaphthoquinonesJournal of cellular physiology
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Insulin-like growth factor 1 differentially regulates estrogen receptor-dependent transcription at estrogen response element and AP-1 sites in breast…

2007

Cross-talk between insulin-like growth factor 1 (IGF-1) and estrogen receptor alpha (ER) regulates gene expression in breast cancer cells, but the underlying mechanisms remain unclear. Here, we studied how 17-beta-estradiol (E2) and IGF-1 affect ER transcriptional machinery in MCF-7 cells. E2 treatment stimulated ER loading on the estrogen response element (ERE) in the pS2 promoter and on the AP-1 motif in the cyclin D1 promoter. On ERE, similar amounts of liganded ER were found at 1-24-h time points, whereas on AP-1, ER binding fluctuated over time. At 1 h, liganded ER was recruited to ERE together with histone acetyltransferases SRC-1 and p300, ubiquitin ligase E6-AP, histone methyltransf…

Transcription GeneticActive Transport Cell NucleusEstrogen receptorBreast NeoplasmsLigandsResponse ElementsBiochemistryCyclin D1Cell Line TumorHumansCyclin D1RNA MessengerInsulin-Like Growth Factor IHistone H3 acetylationMolecular BiologyHormone response elementbiologyEstradiolTumor Suppressor ProteinsEstrogen Receptor alphaCell BiologyUbiquitin ligaseCell biologyUp-RegulationTranscription Factor AP-1Histone methyltransferasebiology.proteinCancer researchMdm2Trefoil Factor-1Estrogen receptor alphahormones hormone substitutes and hormone antagonistsThe Journal of biological chemistry
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Transcriptional Activity and Nuclear Localization of Cabut, the Drosophila Ortholog of Vertebrate TGF-β-Inducible Early-Response Gene (TIEG) Proteins

2011

Background Cabut (Cbt) is a C2H2-class zinc finger transcription factor involved in embryonic dorsal closure, epithelial regeneration and other developmental processes in Drosophila melanogaster. Cbt orthologs have been identified in other Drosophila species and insects as well as in vertebrates. Indeed, Cbt is the Drosophila ortholog of the group of vertebrate proteins encoded by the TGF-s-inducible early-response genes (TIEGs), which belong to Sp1-like/Kruppel-like family of transcription factors. Several functional domains involved in transcriptional control and subcellular localization have been identified in the vertebrate TIEGs. However, little is known of whether these domains and fu…

Transcription GeneticNuclear Localization SignalsActive Transport Cell Nucleuslcsh:MedicineGene ExpressionBiochemistrybehavioral disciplines and activities03 medical and health sciencesModel Organisms0302 clinical medicineTransforming Growth Factor betaMolecular Cell Biologymental disordersGeneticsTranscriptional regulationAnimalsDrosophila Proteinslcsh:ScienceBiology030304 developmental biologyGeneticsZinc finger transcription factor0303 health sciencesMultidisciplinarybiologySchneider 2 cellslcsh:RfungiProteinsAnimal Modelsbiology.organism_classificationFusion proteinCellular StructuresDorsal closure3. Good healthRepressor ProteinsDrosophila melanogasterGene Expression RegulationVertebrateslcsh:QDrosophila melanogaster030217 neurology & neurosurgeryDrosophila ProteinNuclear localization sequenceTranscription FactorsResearch ArticleDevelopmental BiologyPLoS ONE
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Mechanism of leptin expression in breast cancer cells: role of hypoxia-inducible factor-1α

2007

We reported previously that the obesity hormone leptin is overexpressed in breast cancer biopsies. Here, we investigated molecular mechanisms involved in this process, focusing on conditions that are associated with obesity, that is, hyperinsulinemia and induction of hypoxia. By using quantitative real-time PCR, immunofluorescent detection of proteins and enzyme-linked immunosorbent assays, we found that treatment of MCF-7 breast cancer cells with high doses of insulin or the hypoxia-mimetic agent CoCl2, or culturing the cells under hypoxic conditions significantly increased the expression of leptin mRNA and protein. Notably, the greatest leptin mRNA and protein expression were observed und…

Transcriptional ActivationCancer Researchmedicine.medical_specialtyActive Transport Cell NucleusBreast NeoplasmsBiologymedicine.disease_causeleptinbreast cancerInternal medicineCoactivatorGene expressionTumor Cells CulturedGeneticsmedicineHumansInsulinHIFp300-CBP Transcription FactorsPromoter Regions GeneticMolecular BiologyCell NucleusRegulation of gene expressionBinding SitesLeptin receptorLeptinPromoterCobaltHypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaGene Expression Regulation NeoplasticEndocrinologyhyperinsulinemiaCarcinogenesisChromatin immunoprecipitationhormones hormone substitutes and hormone antagonistsProtein BindingOncogene
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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery

2004

12 páginas, 7 figuras, 1 tabla. Material suplementario en: https://doi.org/10.1016/S0092-8674(03)01025-0. The SUS1 sequences have been deposited in GenBank with the accession number AY278445.

Transcriptional ActivationNucleocytoplasmic Transport ProteinsDNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataActive Transport Cell NucleusPorinsRNA polymerase IIBiologyGeneral Biochemistry Genetics and Molecular BiologyFungal ProteinsTranscription (biology)AcetyltransferasesGene Expression Regulation FungalYeastsGene expressionGenes RegulatorTranscriptional regulationAmino Acid SequenceRNA MessengerNuclear proteinPromoter Regions GeneticHistone AcetyltransferasesRegulation of gene expressionCell NucleusBase SequenceBiochemistry Genetics and Molecular Biology(all)Nuclear ProteinsRNA-Binding ProteinsMolecular biologyCell biologySAGA complexRibonucleoproteinsbiology.proteinNuclear PoreGenes LethalChromatin immunoprecipitation
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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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