Search results for "Nuclear Proteins"

showing 10 items of 295 documents

Impaired DNA demethylation of C/EBP sites causes premature aging

2018

Changes in DNA methylation are among the best-documented epigenetic alterations accompanying organismal aging. However, whether and how altered DNA methylation is causally involved in aging have remained elusive. GADD45α (growth arrest and DNA damage protein 45A) and ING1 (inhibitor of growth family member 1) are adapter proteins for site-specific demethylation by TET (ten-eleven translocation) methylcytosine dioxygenases. Here we show that Gadd45a/Ing1 double-knockout mice display segmental progeria and phenocopy impaired energy homeostasis and lipodystrophy characteristic of Cebp (CCAAT/enhancer-binding protein) mutants. Correspondingly, GADD45α occupies C/EBPβ/δ-dependent superenhancers …

0301 basic medicinePremature agingAgingLipodystrophyDNA damageCell Cycle ProteinsBiology03 medical and health sciencesMiceGeneticsAnimalsHomeostasisEpigeneticsCells CulturedDemethylationMice KnockoutNuclear ProteinsAging PrematureMethylationCell biologyChromatinDNA Demethylation030104 developmental biologyDNA demethylationDNA methylationCCAAT-Enhancer-Binding ProteinsInhibitor of Growth Protein 1Developmental BiologyResearch Paper
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Fold formation at the compartment boundary of Drosophila wing requires Yki signaling to suppress JNK dependent apoptosis

2016

AbstractCompartment boundaries prevent cell populations of different lineage from intermingling. In many cases, compartment boundaries are associated with morphological folds. However, in the Drosophila wing imaginal disc, fold formation at the anterior/posterior (A/P) compartment boundary is suppressed, probably as a prerequisite for the formation of a flat wing surface. Fold suppression depends on optomotor-blind (omb). Omb mutant animals develop a deep apical fold at the A/P boundary of the larval wing disc and an A/P cleft in the adult wing. A/P fold formation is controlled by different signaling pathways. Jun N-terminal kinase (JNK) and Yorkie (Yki) signaling are activated in cells alo…

0301 basic medicineProgrammed cell deathanimal structuresMAP Kinase Kinase 4CellMutantApoptosisBiologyArticle03 medical and health sciences0302 clinical medicinemedicineAnimalsDrosophila ProteinsWings AnimalBody PatterningMultidisciplinaryWingKinaseGene Expression Regulation DevelopmentalNuclear ProteinsYAP-Signaling ProteinsAnatomyCell biologyImaginal discDrosophila melanogaster030104 developmental biologymedicine.anatomical_structureImaginal DiscsApoptosisTrans-ActivatorsSignal transduction030217 neurology & neurosurgerySignal TransductionScientific Reports
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Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery

2020

Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. These expansions are responsible for protein misfolding and self-assembly into intranuclear inclusion bodies (IIBs) that are somehow linked to neuronal death. However, owing to lack of a suitable cellular model, the downstream consequences of IIB formation are yet to be resolved. Here, we describe a nuclear protein aggregation model of pathogenic human ataxin-1 and characterize IIB effects. Using an inducible Sleeping Beauty transposon system, we overexpressed the ATXN1(Q82) gene in human mesenchymal stem cells that are resistant to the early cytotoxic effects caused by the expr…

0301 basic medicineSCA1 Spinocerebellar ataxia type-1Intranuclear Inclusion BodiesClinical BiochemistryMSC mesenchymal stem cellProtein aggregationBiochemistry0302 clinical medicineMutant proteinProtein biosynthesisDE differentially expressed genesNuclear proteinlcsh:QH301-705.5FTIR Fourier-transform infrared spectroscopyAtaxin-1lcsh:R5-920biologyChemistryNuclear ProteinspolyQ polyglutamineRibosomeCell biologySB Sleeping BeautyRibosome ; Polyglutamine ; Ataxin-1 ; Oxidative stress ; Transposon ; Sleeping beauty transposon ; Protein networkSpinocerebellar ataxiaProtein foldingCellular modelFunction and Dysfunction of the Nervous Systemlcsh:Medicine (General)Research PaperiPSC induced pluripotent stem cellAtaxin 1Nerve Tissue ProteinsPPI protein-protein interaction03 medical and health sciencesROS reactive oxygen speciesProtein networkSleeping beauty transposonGSEA Gene Set Enrichment AnalysismedicineHumansNPC neural progenitor cellOrganic Chemistrymedicine.diseaseAFM atomic force microscopyOxidative Stress030104 developmental biologylcsh:Biology (General)IIBs intranuclear inclusion bodiesMS mass spectrometryCardiovascular and Metabolic Diseasesbiology.proteinPolyglutamine030217 neurology & neurosurgery
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Cytoplasmic localization of the cell polarity factor scribble supports liver tumor formation and tumor cell invasiveness

2018

The loss of epithelial cell polarity plays an important role in the development and progression of liver cancer. However, the specific molecular mechanisms supporting tumor initiation and progression are poorly understood. In this study, transcriptome data and immunofluorescence stains of tissue samples derived from hepatocellular carcinoma (HCC) patients revealed that overexpression associated with cytoplasmic localization of the baso-lateral cell polarity complex protein Scribble (Scrib) correlated with poor prognosis of HCC patients. In comparison to HCC cells stably expressing wildtype Scrib (ScribWT), mutated Scrib with enforced cytoplasmic enrichment (ScribP305L) induced AKT signaling…

0301 basic medicineSCRIBCytoplasmCarcinoma HepatocellularTumor initiationBiologyMice03 medical and health sciences0302 clinical medicineCell Line TumorCell polarityPhosphoprotein PhosphatasesAnimalsHumansPTENTensinNeoplasm InvasivenessEpithelial–mesenchymal transitionProtein kinase BHepatologyOncogeneTumor Suppressor ProteinsLiver NeoplasmsCell PolarityMembrane ProteinsNuclear ProteinsMolecular biology3. Good healthCell Transformation Neoplastic030104 developmental biologyLiver030220 oncology & carcinogenesisbiology.proteinCancer researchProto-Oncogene Proteins c-aktSignal TransductionHepatology
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Hot1 factor recruits co-activator Sub1 and elongation complex Spt4/5 to osmostress genes.

2016

Hyperosmotic stress response involves the adaptative mechanisms needed for cell survival. Under high osmolarity conditions, many stress response genes are activated by several unrelated transcription factors that are controlled by the Hog1 kinase. Osmostress transcription factor Hot1 regulates the expression of several genes involved in glycerol biosynthesis, and the presence of this transcription factor in their promoters is essential for RNApol II recruitment. The physical association between Hog1 and Hot1 activates this transcription factor and directs the RNA polymerase II localization at these promoters. We, herein, demonstrate that physical and genetic interactions exist between Hot1 …

0301 basic medicineSaccharomyces cerevisiae ProteinsChromosomal Proteins Non-HistoneResponse elementGenes FungalRNA polymerase IISaccharomyces cerevisiaeBiologyBiochemistry03 medical and health sciencesOpen Reading FramesOsmotic PressureRNA Processing Post-TranscriptionalPromoter Regions GeneticMolecular BiologyRNA polymerase II holoenzymeGeneticsGeneral transcription factorNuclear ProteinsPromoterCell BiologyDNA-Binding Proteins030104 developmental biologybiology.proteinTranscription factor II FTranscription factor II ETranscription factor II DTranscriptional Elongation FactorsProtein BindingTranscription FactorsThe Biochemical journal
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The SAGA/TREX‑2 subunit Sus1 binds widely to transcribed genes and affects mRNA turnover globally

2018

Abstract Background Eukaryotic transcription is regulated through two complexes, the general transcription factor IID (TFIID) and the coactivator Spt–Ada–Gcn5 acetyltransferase (SAGA). Recent findings confirm that both TFIID and SAGA contribute to the synthesis of nearly all transcripts and are recruited genome-wide in yeast. However, how this broad recruitment confers selectivity under specific conditions remains an open question. Results Here we find that the SAGA/TREX-2 subunit Sus1 associates with upstream regulatory regions of many yeast genes and that heat shock drastically changes Sus1 binding. While Sus1 binding to TFIID-dominated genes is not affected by temperature, its recruitmen…

0301 basic medicineSaccharomyces cerevisiae Proteinslcsh:QH426-470Transcription GeneticSAGASaccharomyces cerevisiaeBiologySus103 medical and health sciencesTranscripció genèticaTranscription (biology)Stress PhysiologicalGene Expression Regulation FungalCoactivatorGeneticsTranscriptional regulationRNA MessengerPromoter Regions GeneticMolecular BiologyGeneGeneral transcription factorResearchEukaryotic transcriptionNuclear ProteinsRNA-Binding ProteinsRNA FungalCell biologylcsh:Genetics030104 developmental biologyChIP-exoRegulatory sequenceTrans-ActivatorsTranscription factor II DTranscriptionGenèticaProtein BindingGRO
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Visual Working Memory Requires Permissive and Instructive NO/cGMP Signaling at Presynapses in the Drosophila Central Brain.

2017

The gaseous second messenger nitric oxide (NO) has been shown to regulate memory formation by activating retrograde signaling cascades from post- to presynapse that involve cyclic guanosine monophosphate (cGMP) production to induce synaptic plasticity and transcriptional changes. In this study, we analyzed the role of NO in the formation of a visual working memory that lasts only a few seconds. This memory is encoded in a subset of ring neurons that form the ellipsoid body in the Drosophila brain. Using genetic and pharmacological manipulations, we show that NO signaling is required for cGMP-mediated CREB activation, leading to the expression of competence factors like the synaptic homer pr…

0301 basic medicineSerum Response FactorEngramBiologyCREBNitric OxideGeneral Biochemistry Genetics and Molecular BiologyPresynapse03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAnimalsDrosophila ProteinsHydrogen SulfideCyclic guanosine monophosphateCyclic GMPNeuronsNeurotransmitter AgentsWorking memoryNuclear Proteins030104 developmental biologyDrosophila melanogasterMemory Short-TermchemistrySecond messenger systemSynaptic plasticityRetrograde signalingbiology.proteinVisual PerceptionGeneral Agricultural and Biological SciencesNeuroscience030217 neurology & neurosurgerySignal TransductionTranscription FactorsCurrent biology : CB
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The mRNA cap-binding protein Cbc1 is required for high and timely expression of genes by promoting the accumulation of gene-specific activators at pr…

2015

The highly conserved Saccharomyces cerevisiae cap-binding protein Cbc1/Sto1 binds mRNA co-transcriptionally and acts as a key coordinator of mRNA fate. Recently, Cbc1 has also been implicated in transcription elongation and pre-initiation complex (PIC) formation. Previously, we described Cbc1 to be required for cell growth under osmotic stress and to mediate osmostress-induced translation reprogramming. Here, we observe delayed global transcription kinetics in cbc1Δ during osmotic stress that correlates with delayed recruitment of TBP and RNA polymerase II to osmo-induced promoters. Interestingly, we detect an interaction between Cbc1 and the MAPK Hog1, which controls most gene expression c…

0301 basic medicineTBX1Saccharomyces cerevisiae ProteinsTranscription GeneticBiophysicsRNA polymerase IISaccharomyces cerevisiaeBiochemistry03 medical and health sciencesOsmotic PressureStructural BiologyTranscription (biology)Gene Expression Regulation FungalGene expressionGeneticsRNA MessengerMolecular BiologyTranscription factorTranscription Initiation GeneticbiologyActivator (genetics)Nuclear ProteinsPromoterMolecular biology030104 developmental biologyRNA Cap-Binding Proteinsbiology.proteinMitogen-Activated Protein KinasesCREB1Transcription FactorsBiochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
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The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics.

2018

Cytoskeletal dynamics are pivotal to memory, learning, and stress physiology, and thus psychiatric diseases. Downregulated in renal cell carcinoma 1 (DRR1) protein was characterized as the link between stress, actin dynamics, neuronal function, and cognition. To elucidate the underlying molecular mechanisms, we undertook a domain analysis of DRR1 and probed the effects on actin binding, polymerization, and bundling, as well as on actin-dependent cellular processes. Methods: DRR1 domains were cloned and expressed as recombinant proteins to perform in vitro analysis of actin dynamics (binding, bundling, polymerization, and nucleation). Cellular actin-dependent processes were analyzed in trans…

0301 basic medicineTU3ADRR1macromolecular substancesCatalysisArticleInorganic Chemistrylcsh:Chemistryactin dynamics03 medical and health sciencesSerum response factorCitosqueletProteïnes citosquelètiquesFAM107AHumansGenes Tumor SuppressorPhysical and Theoretical ChemistryCytoskeletonMolecular Biologylcsh:QH301-705.5SpectroscopyActinCytoskeletonstress physiologyMicroscopy ConfocalbiologyChemistryOrganic ChemistryFluorescence recovery after photobleachingNuclear ProteinscytoskeletonGeneral Medicinestress physiology ; cytoskeleton ; actin dynamics ; DRR1 ; TU3A ; FAM107AActinsComputer Science ApplicationsCell biologyddc:Cytoskeletal proteinsActinin alpha 1030104 developmental biologyTreadmillingProfilinlcsh:Biology (General)lcsh:QD1-999biology.proteinGelsolinFluorescence Recovery After PhotobleachingHeLa CellsInternational journal of molecular sciences
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Acute depletion of telomerase components DKC1 and NOP10 induces oxidative stress and disrupts ribosomal biogenesis via NPM1 and activation of the P53…

2020

Mutations in DKC1, NOP10, and TINF2 genes, coding for proteins in telomerase and shelterin complexes, are responsible for diverse diseases known as telomeropathies and ribosomopathies, including dyskeratosis congenita (DC, ORPHA 1775). These genes contribute to the DC phenotype through mechanisms that are not completely understood. We previously demonstrated in models of DC that oxidative stress is an early and independent event that occurs prior to telomere shortening. To clarify the mechanisms that induce oxidative stress, we silenced genes DKC1, NOP10, and TINF2 with siRNA technology. With RNA array hybridisation, we found several altered pathways for each siRNA model. Afterwards, we ide…

0301 basic medicineTelomeraseTelomere-Binding ProteinsCell Cycle ProteinsShelterin ComplexCell LineAdherens junction03 medical and health sciences0302 clinical medicineRibonucleoproteins Small NucleolarmedicineRNA Small InterferingMolecular BiologyTelomeraseTelomere ShorteningRibonucleoproteinChemistryRNANuclear ProteinsCell BiologyTelomereShelterinmedicine.diseaseCell biologyTelomereOxidative Stress030104 developmental biology030220 oncology & carcinogenesisMutationTumor Suppressor Protein p53NucleophosminRibosomesDyskeratosis congenitaBiogenesisBiochimica et biophysica acta. Molecular cell research
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