Search results for "Transcription factor"

showing 10 items of 1493 documents

PARD3 Inactivation in Lung Squamous Cell Carcinomas Impairs STAT3 and Promotes Malignant Invasion.

2015

Abstract Correct apicobasal polarization and intercellular adhesions are essential for the appropriate development of normal epithelia. Here, we investigated the contribution of the cell polarity regulator PARD3 to the development of lung squamous cell carcinomas (LSCC). Tumor-specific PARD3 alterations were found in 8% of LSCCs examined, placing PARD3 among the most common tumor suppressor genes in this malignancy. Most PAR3-mutant proteins exhibited a relative reduction in the ability to mediate formation of tight junctions and actin-based protrusions, bind atypical protein kinase C, activate RAC1, and activate STAT3 at cell confluence. Thus, PARD3 alterations prevented the formation of c…

STAT3 Transcription Factorrac1 GTP-Binding ProteinCancer ResearchLung NeoplasmsCellMice NudeRAC1Cell Cycle ProteinsBiologyArticleCell MovementCell Line TumorCell polaritymedicineAnimalsHumansNeoplasm InvasivenessProtein Kinase CAdaptor Proteins Signal TransducingCell ProliferationConfluencyTight junctionBase SequenceCell growthLiver NeoplasmsMembrane ProteinsSequence Analysis DNACell biologymedicine.anatomical_structureOncologyCell cultureMutationCancer researchCarcinoma Squamous CellTranscriptomeIntracellularNeoplasm TransplantationCancer research
researchProduct

Novel Signal Transduction Pathways: Analysis of STAT-3 and Rac-1 Signaling in Inflammatory Bowel Disease

2006

Although the precise etiology of inflammatory bowel disease still remains unclear, considerable progress has been made in the identification of novel signal transduction pathways that elucidate the immunopathogenesis involved in the perpetuation of the inflammatory process. Augmented T cell resistance against apoptosis is regarded as a pivotal factor in the pathogenesis, as it impairs mucosal homeostasis and leads to unrestrained accumulation of activated T cells, which subsequently lead to the amplification of the inflammatory response. Therefore novel therapeutic strategies aim at restoring mucosal T cell susceptibility to apoptosis through targeting of signal transduction pathways that a…

STAT3 Transcription Factorrac1 GTP-Binding ProteinT-LymphocytesT cellApoptosisTherapeutic ProcedureAzathioprineBiologyInflammatory bowel diseaseGeneral Biochemistry Genetics and Molecular BiologystatPathogenesisHistory and Philosophy of ScienceAzathioprinemedicineHumansGeneral NeuroscienceInflammatory Bowel Diseasesmedicine.diseasemedicine.anatomical_structureApoptosisImmunologySignal transductionImmunosuppressive AgentsSignal Transductionmedicine.drugAnnals of the New York Academy of Sciences
researchProduct

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
researchProduct

The MAPK Hog1 recruits Rpd3 histone deacetylase to activate osmoresponsive genes

2003

Regulation of gene expression by mitogen-activated protein kinases (MAPKs) is essential for proper cell adaptation to extracellular stimuli. Exposure of yeast cells to high osmolarity results in rapid activation of the MAPK Hog1, which coordinates the transcriptional programme required for cell survival on osmostress. The mechanisms by which Hog1 and MAPKs in general regulate gene expression are not completely understood, although Hog1 can modify some transcription factors. Here we propose that Hog1 induces gene expression by a mechanism that involves recruiting a specific histone deacetylase complex to the promoters of genes regulated by osmostress. Cells lacking the Rpd3-Sin3 histone deac…

Saccharomyces cerevisiae ProteinsGenes FungalSaccharomyces cerevisiaeBiologySAP30Histone DeacetylasesOsmotic PressureGene Expression Regulation FungalPromoter Regions GeneticOligonucleotide Array Sequence AnalysisHistone deacetylase 5MultidisciplinaryHistone deacetylase 2HDAC11HDAC10HDAC9Molecular biologyHDAC4Cell biologyRepressor ProteinsMutationHistone deacetylase complexRNA Polymerase IIMitogen-Activated Protein KinasesProtein BindingTranscription FactorsNature
researchProduct

Expression of a Truncated Yeast Ccc1 Vacuolar Transporter Increases the Accumulation of Endogenous Iron

2021

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox cofactor in multiple metabolic processes. Iron bioavailability is highly restricted due to the low solubility of its oxidized form, frequently leading to iron deficiency anemia. The baker’s yeast Saccharomyces cerevisiae is used as a model organism for iron homeostasis studies, but also as a food supplement and fermentative microorganism in the food industry. Yeast cells use the vacuolar Ccc1 transporter to detoxify and store excess iron in the vacuoles. Here, we modulate CCC1 expression and properties to increase iron extraction from the environment. We show that constitutive expression of fu…

Saccharomyces cerevisiae ProteinsIronSaccharomyces cerevisiaeCcc1EndogenyVacuoleSaccharomyces cerevisiaeyeastQH426-470CofactorArticle<i>Saccharomyces cerevisiae</i>03 medical and health sciencesironWestern blotGene Expression Regulation FungalmedicineGeneticsTranscription factorCation Transport ProteinsGenetics (clinical)030304 developmental biology0303 health sciencesmedicine.diagnostic_testbiology030306 microbiologyChemistryBiological Transportbiology.organism_classificationYeastYeastCell biologyCytosolVacuolesbiology.proteinGenes
researchProduct

Functional Connection Between the Clb5 Cyclin, the Protein Kinase C Pathway and the Swi4 Transcription Factor in Saccharomyces cerevisiae

2005

Abstract The rsf12 mutation was isolated in a synthetic lethal screen for genes functionally interacting with Swi4. RSF12 is CLB5. The clb5 swi4 mutant cells arrest at G2/M due to the activation of the DNA-damage checkpoint. Defects in DNA integrity was confirmed by the increased rates of chromosome loss and mitotic recombination. Other results suggest the presence of additional defects related to morphogenesis. Interestingly, genes of the PKC pathway rescue the growth defect of clb5 swi4, and pkc1 and slt2 mutations are synthetic lethal with clb5, pointing to a connection between Clb5, the PKC pathway, and Swi4. Different observations suggest that like Clb5, the PKC pathway and Swi4 are in…

Saccharomyces cerevisiae ProteinsMitotic crossoverBlotting WesternMutantSaccharomyces cerevisiaeSaccharomyces cerevisiaeInvestigationsCyclin BBiologymedicine.disease_causeGeneticsmedicineHydroxyureaImmunoprecipitationDNA FungalFluorescent Antibody Technique IndirectTranscription factorProtein Kinase CProtein kinase CCyclinRecombination GeneticGeneticsMutationKinaseCell CyclefungiFlow Cytometrybiology.organism_classificationMolecular biologyCell biologyDNA-Binding ProteinsMutationChromosomes FungalTranscription FactorsGenetics
researchProduct

Regulation of mating in the budding yeast Saccharomyces cerevisiae by the zinc cluster proteins Sut1 and Sut2

2013

This article is made available through the Brunel Open Access Publishing Fund. Copyright @ The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The zinc cluster proteins Sut1 and Sut2 play a role in sterol uptake and filamentous growth in the budding yeast Saccharomyces cerevisiae. In this study, we show that they are also involved in mating. Cells that lack both SUT1 and SUT2 were defective in mating. The expression of the genes NCE102 and PRR2 was increased in the sut1 sut2 double deletion mutant…

Saccharomyces cerevisiae ProteinsMonosaccharide Transport ProteinsSaccharomyces cerevisiaeBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryFungal ProteinsGene Expression Regulation FungalReproduction AsexualBudding yeastMatingMolecular BiologyGenereproductive and urinary physiologyGeneticsMatingZinc FingersCell Biologybiology.organism_classificationBudding yeastSut2Sut1Mating of yeastPheromone responseZinc cluster proteinsZinc Clusterbehavior and behavior mechanismsPheromoneTranscription FactorsSterol uptakeBiochemical and Biophysical Research Communications
researchProduct

Cooperation of Two mRNA-Binding Proteins Drives Metabolic Adaptation to Iron Deficiency

2008

Summary Iron (Fe) is an essential cofactor for a wide range of cellular processes. We have previously demonstrated in yeast that Cth2 is expressed during Fe deficiency and promotes degradation of a battery of mRNAs leading to reprogramming of Fe-dependent metabolism and Fe storage. We report here that the Cth2-homologous protein Cth1 is transiently expressed during Fe deprivation and participates in the response to Fe deficiency through the degradation of mRNAs primarily involved in mitochondrially localized activities including respiration and amino acid biosynthesis. In parallel, wild-type cells, but not cth1 Δ cth2 Δ cells, accumulate mRNAs encoding proteins that function in glucose impo…

Saccharomyces cerevisiae ProteinsPhysiologySaccharomyces cerevisiaeHUMDISEASERNA-binding proteinSaccharomyces cerevisiaeProtein Serine-Threonine KinasesDNA-binding proteinArticlechemistry.chemical_compoundTristetraprolinGlucose importRNA MessengerPhosphorylationProtein kinase AMolecular BiologybiologyGlycogenRNA-Binding ProteinsIron DeficienciesCell BiologyMetabolismbiology.organism_classificationAdaptation PhysiologicalDNA-Binding ProteinsMetabolismBiochemistrychemistryPhosphorylationTranscription FactorsCell Metabolism
researchProduct

Protein Interactions within the Set1 Complex and Their Roles in the Regulation of Histone 3 Lysine 4 Methylation

2006

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc…

Saccharomyces cerevisiae ProteinsProtein subunitLysineRNA polymerase IISaccharomyces cerevisiaeMethylationenvironment and public healthBiochemistryProtein–protein interactionHistonesSerineGene Expression Regulation FungalCoding regionMolecular BiologybiologyLysineHistone-Lysine N-MethyltransferaseCell BiologyMethylationDNA-Binding ProteinsProtein SubunitsHistoneBiochemistrybiology.proteinProtein BindingTranscription FactorsJournal of Biological Chemistry
researchProduct

Bromodomain factor 1 (Bdf1) protein interacts with histones

2001

AbstractUsing a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1–59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304–571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and H4 having different degrees of acetylation. Finally, we have not detected histone acetyltransferase activity associated with Bdf1p.

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsBiophysicsBromodomainTwo-hybridBiochemistryFungal ProteinsHistonesHistone H4SaccharomycesAcetyltransferasesGenes ReporterStructural BiologyTwo-Hybrid System TechniquesHistone methylationHistone H2AGeneticsHistone acetyltransferase activityHistone octamerMolecular BiologyHistone AcetyltransferasesBromodomain factor 1 proteinbiologyChemistryCell BiologyHistone acetyltransferasePeptide FragmentsChromatinBromodomainHistoneBiochemistryPCAFbiology.proteinHistone acetyltransferaseProtein BindingTranscription FactorsFEBS Letters
researchProduct