Search results for "Co-Repressor Proteins"

showing 6 items of 6 documents

Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2

2002

AbstractNuclear domains (ND) 10 are associated with proteins implicated in transcriptional regulation, growth suppression, and apoptosis. We now show that the minor capsid protein L2 of human papillomavirus (HPV) type 33 induces a reorganization of ND10-associated proteins. Whereas the promyelocytic leukemia protein, the major structural component of ND10, was unaffected by L2, Sp100 was released from ND10 upon L2 expression. The total cellular amount of Sp100, but not of Sp100 mRNA, decreased significantly, suggesting degradation of Sp100. Proteasome inhibitors induced the dispersal of Sp100 and inhibited the nuclear translocation of L2. In contrast to Sp100, Daxx was recruited to ND10 by …

Co-Repressor ProteinsImmunoprecipitationFluorescent Antibody TechniqueVaccinia virusPromyelocytic Leukemia ProteinAutoantigenspapillomavirusCell LinePromyelocytic leukemia proteinCapsidDeath-associated protein 6DaxxVirologyHumansSp100RNA MessengerAdaptor Proteins Signal TransducingCell NucleusRecombination GeneticbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsND10Signal transducing adaptor proteinAntigens NuclearOncogene Proteins ViralL2biochemical phenomena metabolism and nutritionBlotting NorthernMolecular biologyNeoplasm ProteinsTransport proteinCell biologyProtein TransportProteasomeCapsidbiology.proteinRNACapsid ProteinsFemaleCarrier ProteinsCo-Repressor ProteinsMolecular ChaperonesTranscription FactorsVirology
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Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 an…

2003

Nuclear domains called ND10 or PML bodies might function as nuclear depots by recruiting or releasing certain proteins. Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences. Exposure to sublethal environmental stress revealed a sequential release of ND10-associated proteins. Upon heat shock Daxx and Sp100 were released but PML remained, whereas exposure to subtoxic concentrations of CdCl2 induced the release of ND10-associated proteins, including PML, with Sp100 remaining in a few sites. In both cases,recovery times were simil…

Co-Repressor ProteinsMAP Kinase Signaling SystemMacromolecular SubstancesSUMO-1 ProteinPromyelocytic Leukemia ProteinMicePromyelocytic leukemia proteinDeath-associated protein 6Stress PhysiologicalHeat shock proteinEndopeptidasesAnimalsHSP70 Heat-Shock ProteinsEnzyme InhibitorsHeat shockTranscription factorCells CulturedHeat-Shock ProteinsbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsCell BiologyCell Nucleus StructuresNeoplasm ProteinsCell biologyHsp70Cysteine EndopeptidasesEukaryotic CellsGene Expression RegulationImmunologybiology.proteinSignal transductionCarrier ProteinsCo-Repressor ProteinsHeat-Shock ResponseCadmiumMolecular ChaperonesTranscription FactorsJournal of Cell Science
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The Co‐mutational Spectrum Determines the Therapeutic Response in Murine FGFR2 Fusion‐Driven Cholangiocarcinoma

2021

Background and aims Intrahepatic cholangiocarcinoma (ICC) is the second most common primary liver cancer and a highly lethal malignancy. Chemotherapeutic options are limited, but a considerable subset of patients harbors genetic lesions for which targeted agents exist. Fibroblast growth factor receptor 2 (FGFR2) fusions belong to the most frequent and therapeutically relevant alterations in ICC, and the first FGFR inhibitor was recently approved for the treatment of patients with progressed, fusion-positive ICC. Response rates of up to 35% indicate that FGFR-targeted therapies are beneficial in many but not all patients. Thus far, no established biomarkers exist that predict resistance or r…

Fetal Proteins0301 basic medicineAntimetabolites AntineoplasticCombination therapymedicine.medical_treatmentFGFR InhibitionVesicular Transport ProteinsCyclic AMP Response Element-Binding Protein Amedicine.disease_causeDeoxycytidineMalignant transformationTargeted therapyCholangiocarcinomaProto-Oncogene Proteins p21(ras)Mice03 medical and health sciencesLiver Neoplasms Experimental0302 clinical medicineAntigens NeoplasmmedicineAnimalsReceptor Fibroblast Growth Factor Type 2Protein Kinase InhibitorsCell ProliferationHepatologyOncogenebusiness.industryFibroblast growth factor receptor 2AdenosylhomocysteinasePhenylurea CompoundsGemcitabineBile Ducts IntrahepaticCell Transformation NeoplasticPyrimidines030104 developmental biologyBile Duct NeoplasmsFibroblast growth factor receptorMutationCancer research030211 gastroenterology & hepatologyKRASGene FusionbusinessCo-Repressor ProteinsMicrotubule-Associated ProteinsHepatology
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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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Gene expression in mouse spermatogenesis during ontogenesis

2006

In this study, we evaluated the expression of genes probably involved in spermatogenesis in the mouse. We examined cytosolic chaperonin theta subunit (CCTtheta), Ngg1 interacting factor 3 like 1 binding protein 1 (NIF3L1 BP1) and apolipoprotein H (ApoH) expression during mouse onto-geny using RT-PCR. Testicular tissue was obtained from mice 3, 6, 8, 10, 12, 14, 18, 20 and 40 (adult) days after birth. For each mouse, one testis was used for histological examination, whereas RNA was extracted from the controlateral testis for expression analysis. RT-PCR analysis showed that CCTtheta gene expression was low until day 10, but increased drastically afterwards. At this age, spermatocytes started …

MaleChaperoninsSpermiogenesisMouse testis ontogenesisBiologyMiceGene expressionTestisGeneticsmedicineAnimalsRNA MessengerSpermatogenesisGeneGene expression; Mouse testis ontogenesis; SpermatogenesisGlycoproteinsReverse Transcriptase Polymerase Chain ReactionGene Expression Regulation DevelopmentalProteinsGeneral MedicineCell cycleMolecular biologyCell biologyChromatinmedicine.anatomical_structurebeta 2-Glycoprotein IGene expressionSpermatogenesisApolipoprotein HCo-Repressor ProteinsGerm cell: gene expression mouse testis ontogenesis spermatogenesisChaperonin Containing TCP-1Transcription Factors
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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