Search results for "ACTIVATOR"

showing 10 items of 488 documents

Avian Clock gene polymorphism: evidence for a latitudinal cline in allele frequencies

2007

In comparison with most animal behaviours, circadian rhythms have a well-characterized molecular genetic basis. Detailed studies of circadian clock genes in 'model' organisms provide a foundation for interpreting the functional and evolutionary significance of polymorphic circadian clock genes found within free-living animal populations. Here, we describe allelic variation in a region of the avian Clock orthologue which encodes a functionally significant polyglutamine repeat (ClkpolyQcds), within free-living populations of two passerine birds, the migratory bluethroat (Luscinia svecica) and the predominantly nonmigratory blue tit (Cyanistes caeruleus). Multiple ClkpolyQcds alleles were foun…

SELECTIONINSTABILITYPREFERENCEMolecular Sequence DataPopulationCLOCK ProteinsLocus (genetics)BiologypolymorphismSexual Behavior AnimalGene FrequencyCyanistesGenotypeLOCUSGeneticsAnimalsLusciniaAmino Acid SequencePasseriformesAlleleeducationAllele frequencyPOPULATIONEcology Evolution Behavior and SystematicsGeneticseducation.field_of_studyPolymorphism GeneticSEQUENCESGeographyCyanistesTIT PARUS-CAERULEUSCline (biology)biology.organism_classificationEVOLUTIONCircadian RhythmCLOCKclockcircadianCIRCADIAN CLOCKSDROSOPHILA-MELANOGASTEREvolutionary biologyTrans-ActivatorspolyglutamineSequence AlignmentMicrosatellite RepeatsMolecular Ecology
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SERCA activity is reduced in DJ-1 mutant flies and human cells due to oxidative modification

2020

ABSTRACTDJ-1 is a causative gene for familial Parkinson’s disease (PD) with different functions, standing out its role against oxidative stress (OS). Accordingly, PD model flies harboring a mutation in the DJ-1β gene (the Drosophila ortholog of human DJ-1) show high levels of OS markers like protein carbonylation, a common post-translational modification that may alter protein function. To increase our understanding of PD pathogenesis as well as to discover potential therapeutic targets for pharmacological intervention, we performed a redox proteomic assay in DJ-1β mutant flies. Among the proteins that showed increased carbonylation levels in PD model flies, we found SERCA, an endoplasmic r…

SERCAChemistryActivator (genetics)Endoplasmic reticulumProtein CarbonylationMutantmedicineOxidative phosphorylationmedicine.disease_causeOxidative stressHomeostasisCell biology
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Cytoplasmic STAT proteins associate prior to activation

2000

The commonly accepted model of STAT factor activation at the cytoplasmic part of the receptor assumes that signal transducers and activators of transcription (STATs) are recruited from a cytoplasmic pool of monomeric STAT proteins. Based on a previous observation that non-phosphorylated STAT3-Src homology 2 domains dimerize in vitro, we investigated whether the observed dimerization is of physiological relevance within the cellular context. We show that STAT1 and STAT3 are pre-associated in non-stimulated cells. Apparently, these complexes are not able to translocate into the nucleus. We provide evidence that the event of STAT activation is more complex than previously assumed.

STAT3 Transcription FactorCytoplasmCarcinoma HepatocellularMolecular Sequence DataCross ReactionsTransfectionCytoplasmic partBiochemistrystatTumor Cells CulturedAnimalsHumansProtein inhibitor of activated STATAmino Acid SequenceSTAT1PhosphorylationSTAT3MelanomaMolecular BiologySTAT4STAT6biologyInterleukin-6Liver NeoplasmsCell BiologyPrecipitin TestsMolecular biologyCell biologyDNA-Binding ProteinsSTAT1 Transcription FactorCOS CellsTrans-Activatorsbiology.proteinSTAT proteinTyrosineDimerizationResearch ArticleBiochemical Journal
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Nitric Oxide-Releasing Drug Glyceryl Trinitrate Targets JAK2/STAT3 Signaling, Migration and Invasion of Triple-Negative Breast Cancer Cells

2021

Triple-negative breast cancer (TNBC) is a highly aggressive disease with invasive and metastasizing properties associated with a poor prognosis. The STAT3 signaling pathway has shown a pivotal role in cancer cell migration, invasion, metastasis and drug resistance of TNBC cells. IL-6 is a main upstream activator of the JAK2/STAT3 pathway. In the present study we examined the impact of the NO-donor glyceryl trinitrate (GTN) on the activation of the JAK2/STAT3 signaling pathway and subsequent migration, invasion and metastasis ability of TNBC cells through in vitro and in vivo experiments. We used a subtoxic dose of carboplatin and/or recombinant IL-6 to activate the JAK2/STAT3 signaling path…

STAT3 Transcription FactorQH301-705.5Triple Negative Breast NeoplasmsmigrationArticleCatalysisStat3 Signaling PathwayMetastasisInorganic ChemistryMiceNitroglycerinchemistry.chemical_compoundCell Movementnitric oxideIn vivoCell Line TumormedicineAnimalsHumanscancermetastasisNeoplasm InvasivenessNitric Oxide DonorsBiology (General)Physical and Theoretical ChemistrySTAT3QD1-999Molecular BiologySpectroscopyTriple-negative breast cancerMice Inbred BALB CbiologyActivator (genetics)Organic ChemistryCancerGeneral MedicineJanus Kinase 2invasionmedicine.diseaseCarboplatinComputer Science ApplicationsChemistrychemistrybiology.proteinCancer researchFemalesignalingSignal TransductionInternational Journal of Molecular Sciences
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Combined interleukin 6 and soluble interleukin 6 receptor accelerates murine liver regeneration.

2000

Abstract Background & Aims: Liver regeneration after loss of hepatic tissue leads to hepatocyte and nonparenchymal cell proliferation and rapid restoration of liver parenchyma. Interleukin (IL)-6 is a key inducer of transcription factors involved in liver regeneration. Whenever IL-6 activates target cells, it binds to a specific IL-6 receptor (IL-6R). The IL-6/IL-6R complex then associates with the signal transducer gp130, leading to activation of intracellular signaling. Methods: We have recently constructed the designer cytokine Hyper-IL-6 consisting of soluble IL-6R covalently linked to IL-6, which directly stimulates gp130 even in the absence of membrane-bound IL-6R. We compared the inf…

STAT3 Transcription FactorTime Factorsmedicine.medical_treatmentMicemedicineAnimalsHepatectomyHumansPostoperative PeriodPhosphorylationInterleukin 6HepatologybiologyInterleukin-6Regeneration (biology)GastroenterologyInterleukinOrgan SizeGlycoprotein 130Receptors Interleukin-6Liver regenerationLiver RegenerationDNA-Binding ProteinsMice Inbred C57BLmedicine.anatomical_structureGene Expression RegulationLiverSolubilityHepatocyteInterleukin-6 receptorImmunologybiology.proteinCancer researchTrans-ActivatorsHepatectomyCell DivisionGastroenterology
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Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptio…

2002

The subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes, is modulated by carbon source availability. In cells growing in glucose, Msn2 is located mainly in the cytosol, whereas in carbon source-starved cells, Msn2 is located largely inside the nucleus. However, in cells lacking Reg1 (the regulatory subunit of the Reg1/Glc7 protein phosphatase complex), the regulation of subcellular distribution is absent, Msn2 being constitutively present in the cytosol. The localization defect in these mutants is specific for carbon starvation stress, and it is because of the presence of an abnormally active Snf1 protein kinase that inhibits the n…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeMitogen-activated protein kinase kinaseBiologyProtein Serine-Threonine KinasesBiochemistryASK1Molecular BiologyDNA PrimersSirolimusMAP kinase kinase kinaseBase SequenceKinaseCell BiologySubcellular localizationCarbonCell biologyCulture MediaDNA-Binding ProteinsCytosolBiochemistryTrans-ActivatorsCyclin-dependent kinase 9Nuclear localization sequenceSubcellular FractionsTranscription FactorsThe Journal of biological chemistry
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Specific Defects in Different Transcription Complexes Compensate for the Requirement of the Negative Cofactor 2 Repressor in Saccharomyces cerevisiae

2007

Abstract Negative cofactor 2 (NC2) has been described as an essential and evolutionarily conserved transcriptional repressor, although in vitro and in vivo experiments suggest that it can function as both a positive and a negative effector of transcription. NC2 operates by interacting with the core promoter and components of the basal transcription machinery, like the TATA-binding protein (TBP). In this work, we have isolated mutants that suppress the growth defect caused by the depletion of NC2. We have identified mutations affecting components of three different complexes involved in the control of basal transcription: the mediator, TFIIH, and RNA pol II itself. Mutations in RNA pol II in…

Saccharomyces cerevisiae ProteinsTranscription GeneticRepressorRNA polymerase IISaccharomyces cerevisiaeInvestigationsGeneticsPromoter Regions GeneticTranscription factorAllelesGeneticsAdenosine TriphosphatasesTATA-Binding Protein Associated FactorsbiologyGeneral transcription factorDNA HelicasesPromoterPhosphoproteinsRepressor ProteinsProtein SubunitsTranscription Factor TFIIHMutationTranscription factor II Hbiology.proteinTrans-ActivatorsTranscription Factor TFIIBMutant ProteinsTranscription Factor TFIIDRNA Polymerase IITranscription factor II BTranscription Factor TFIIHTranscription Factors
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Urmylation and tRNA thiolation functions of ubiquitin-like Uba4·Urm1 systems are conserved from yeast to man

2015

AbstractThe ubiquitin-like protein Urm1 from budding yeast and its E1-like activator Uba4 have dual roles in protein urmylation and tRNA thiolation pathways. To study whether these are conserved among eukaryotes, we used gene shuffles to replace the yeast proteins by their human counterparts, hURM1 and hUBA4/MOCS3. As judged from biochemical and genetical assays, hURM1 and hUBA4 are functional in yeast, albeit at reduced efficiencies. They mediate urmylation of the peroxiredoxin Ahp1, a known urmylation target in yeast, and support tRNA thiolation. Similar to hUBA4, yeast Uba4 itself is modified by Urm1 and hURM1 suggesting target overlap between eukaryal urmylation pathways. In sum, our st…

Saccharomyces cerevisiae ProteinsUba4 (hUBA4/MOCS3)Saccharomyces cerevisiaeBiophysicstRNA thiolationSaccharomyces cerevisiaeBiochemistryUbiquitin-like urmylationRNA TransferUbiquitinStructural BiologyAnticodonGeneticsHumansUbiquitinsMolecular BiologyProtein urmylationGeneUrm1 (hURM1)Conserved SequenceSequence Homology Amino AcidbiologyActivator (genetics)TRNA thiolationCell Biologybiology.organism_classificationNucleotidyltransferasesYeastBiochemistrySulfurtransferasesbiology.proteinPeroxiredoxinHeLa CellsFEBS Letters
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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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The critical concentration of C1-esterase inhibitor (C1-INH) in human serum preventing auto-activation of the first component of complement (C1)

2005

C1-esterase inhibitor (C1-INH) was depleted from normal human serum (NHS) at 4 degrees C by affinity chromatography with a monoclonal anti-C1-INH antibody (mAb 13 E1) coupled to CNBr-activated Sepharose 4B. The C1-INH-depleted serum (C1-INH-depl-HS) had normal levels of C1, C4, and CH 50 and C1-INH concentration was less than 10% of normal (15 microg/ml in C1-INH-depl-HS compared to 230 microg/ml in NHS). C1-auto-activation in C1-INH-depl-HS was followed by measuring C4-consumption in a haemolytic assay and by detection of activated C1s in a C1s-ELISA. After a lag phase of 10-20 min, C1-auto-activation in C1-INH depl-HS occurred and reached its maximum after 40 min at 37 degrees C. In contr…

Serummedicine.drug_classImmunologyComplement C1 Inactivator ProteinsMonoclonal antibodyNeutralizationSepharoseMiceAffinity chromatographyComplement C1medicineAnimalsHumansheterocyclic compoundsMolecular BiologybiologyChemistryAntibodies Monoclonalbiochemical phenomena metabolism and nutritionrespiratory systembacterial infections and mycosesMolecular biologyrespiratory tract diseasesC1 esteraseComplement C1 Inactivator ProteinsBiochemistryMonoclonalbiology.proteinAntibodyMolecular Immunology
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