Search results for "Corepressor"

showing 6 items of 6 documents

The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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In vivo GSH depletion induces c-myc expression by modulation of chromatin protein complexes.

2009

Abstract We hypothesize that glutathione (GSH) fluctuations could have a prominent role in the modulation of c-myc expression through a mechanism affecting chromatin remodeling complexes. This could lead to an open chromatin structure accessible to transcription factors. We studied the in vivo effect of GSH depletion on these complexes bound to the c-myc promoter in the liver of l-buthionine-(S,R)-sulfoximine (BSO)-treated rats. Using chromatin immunoprecipitation we found that 3 h after BSO treatment the repressing complexes Id2 and Sin3A (part of a histone–deacetylase complex) were released from the c-myc promoter. STAT3 was phosphorylated and associated with its coactivator p300 with int…

MaleSTAT3 Transcription FactorTranscriptional ActivationTime FactorsBiologyBiochemistryChromatin remodelingHistone DeacetylasesProto-Oncogene Proteins c-mycHistone H3Physiology (medical)Gene expressionCoactivatorTranscriptional regulationAnimalsp300-CBP Transcription FactorsPhosphorylationRats WistarTranscription factorButhionine SulfoximineInhibitor of Differentiation Protein 2AcetylationChromatin Assembly and DisassemblyMolecular biologyGlutathioneChromatinRatsRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexGene Expression RegulationLiverChromatin immunoprecipitationProtein BindingFree radical biologymedicine
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SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus.

2006

Histone acetylation plays a key role in the regulation of gene expression. The chromatin structure and accessibility of genes to transcription factors is regulated by enzymes that acetylate and deacetylate histones. The Sin3A corepressor complex recruits histone deacetylases and in many cases represses transcription. Here, we report that SAP30L, a close homolog of Sin3-associated protein 30 (SAP30), interacts with several components of the Sin3A corepressor complex. We show that it binds to the PAH3/HID (Paired Amphipathic Helix 3/Histone deacetylase Interacting Domain) region of mouse Sin3A with residues 120–140 in the C-terminal part of the protein. We provide evidence that SAP30L induces…

entsyymitvuorovaikutustumajyvänenBiologySAP30Protein Sorting SignalsHistone DeacetylasesArticleCell Line03 medical and health sciencesMice0302 clinical medicineHistone H1Histone H2AGeneticsHistone codeAnimalsHumansGene Silencingnucleolus030304 developmental biologyNuclear receptor co-repressor 2Histone deacetylationGenetics0303 health sciencesgeenitbiokemiaNuclear ProteinsCell biologyRepressor ProteinsProtein TransportSin3 Histone Deacetylase and Corepressor Complextranskriptio (biologia)030220 oncology & carcinogenesisSin-associated proteinsHistone deacetylase complexhistonideasetylaatioHistone deacetylaseproteiinitCorepressorSin-assosioituvat proteiinitCell NucleolusNucleic acids research
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The Use and Abuse of LexA by Mobile Genetic Elements

2016

The SOS response is an essential process for responding to DNA damage in bacteria. The expression of SOS genes is under the control of LexA, a global transcription factor that undergoes self-cleavage during stress to allow the expression of DNA repair functions and delay cell division until the damage is rectified. LexA also regulates genes that are not part of this cell rescue program, and the induction of bacteriophages, the movement of pathogenicity islands, and the expression of virulence factors and bacteriocins are all controlled by this important transcription factor. Recently it has emerged that when regulating the expression of genes from mobile genetic elements (MGEs), LexA often …

0301 basic medicineMicrobiology (medical)Transcription GeneticDNA repair030106 microbiologyRegulatorBiologyRegulonMicrobiology03 medical and health sciencesBacterial ProteinsVirologyGene expressionBacteriophagesSOS responseSOS Response GeneticsTranscription factorGeneGeneticsSerine Endopeptidasesbiochemical phenomena metabolism and nutritionInterspersed Repetitive Sequencesenzymes and coenzymes (carbohydrates)Infectious DiseasesbacteriaRepressor lexACorepressorDNA DamageTrends in Microbiology
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Genetic identification of a network of factors that functionally interact with the nucleosome remodeling ATPase ISWI.

2008

Nucleosome remodeling and covalent modifications of histones play fundamental roles in chromatin structure and function. However, much remains to be learned about how the action of ATP-dependent chromatin remodeling factors and histone-modifying enzymes is coordinated to modulate chromatin organization and transcription. The evolutionarily conserved ATP-dependent chromatin-remodeling factor ISWI plays essential roles in chromosome organization, DNA replication, and transcription regulation. To gain insight into regulation and mechanism of action of ISWI, we conducted an unbiased genetic screen to identify factors with which it interacts in vivo. We found that ISWI interacts with a network o…

MaleProteomicsCancer Researchlcsh:QH426-470Histone Deacetylase 1BiologySettore MED/08 - Anatomia PatologicaChromosomesHistone DeacetylasesChromatin remodelingHistonesHistone H403 medical and health sciences0302 clinical medicineGenetics and Genomics/EpigeneticsGeneticsAnimalsDrosophila ProteinsNucleosomeMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and Systematics030304 developmental biologyAdenosine TriphosphatasesGenetics0303 health sciencesNuclear ProteinsAcetylationChromatin Assembly and DisassemblyChromatinNucleosomesChromatiniswi drosophilaRepressor ProteinsChromatin epigeneticsHDAC Chromatin RemodellingSin3 Histone Deacetylase and Corepressor Complexlcsh:GeneticsDrosophila melanogasterHistoneHistone deacetylase complexbiology.proteinFemaleHistone deacetylaseHistone deacetylase activity030217 neurology & neurosurgeryResearch ArticleTranscription Factors
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Synthetic retinoids dissociate coactivator binding from corepressor release.

2002

The ligand-activated retinoid receptors RXR and RAR control development, homeostasis and disease by regulating transcription of retinoic acid (RA) responsive target genes or crosstalk with other signalling pathways. According to the current model ligand-binding triggers an exchange between corepressor- and coactivator-complexes that inhibit or potentiate transcription by deacetylating and acetylating nucleosomal histones, respectively. Additional cofactors may modify the transcriptional regulatory process by linking liganded retinoid receptors to structural components of chromatin or protein degradation. The desire to specifically influence defined events in RA-signalling, while others are …

Transcriptional Activationmedicine.drug_classReceptors Retinoic AcidAmino Acid MotifsProtein degradationRetinoid X receptorBiologyLigandsBiochemistryRetinoidsCoactivatorChlorocebus aethiopsmedicineAnimalsHumansNuclear Receptor Co-Repressor 1Protein IsoformsNuclear Receptor Co-Repressor 2RetinoidMolecular BiologyNuclear receptor co-repressor 2PELP-1Binding SitesRetinoid X receptor alphaRetinoic Acid Receptor alphaNuclear ProteinsCell BiologyCell biologyDNA-Binding ProteinsRepressor ProteinsBiochemistryGene Expression RegulationCOS CellsMutagenesis Site-DirectedCorepressorHeLa CellsJournal of receptor and signal transduction research
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