Search results for "subcellular localization"

showing 10 items of 53 documents

Chimeric proteins tagged with specific 3xHA cassettes may present instability and functional problems

2017

Epitope-tagging of proteins has become a widespread technique for the analysis of protein function, protein interactions and protein localization among others. Tagging of genes by chromosomal integration of PCR amplified cassettes is a widely used and fast method to label proteins in vivo. Different systems have been developed during years in the yeast Saccharomyces cerevisiae. In the present study, we analysed systematically a set of yeast proteins that were fused to different tags. Analysis of the tagged proteins revealed an unexpected general effect on protein level when some specific tagging module was used. This was due in all cases to a destabilization of the proteins and caused a red…

0301 basic medicinePhysiologyProtein Extractionlcsh:MedicineYeast and Fungal ModelsPolymerase Chain ReactionBiochemistryGreen fluorescent proteinEpitopesDatabase and Informatics MethodsGene Expression Regulation FungalImmune PhysiologyProtein purificationMacromolecular Structure AnalysisMedicine and Health SciencesProto-Oncogene Proteins c-myclcsh:ScienceStainingExtraction TechniquesImmune System ProteinsMultidisciplinarybiologyGene targetingProtein subcellular localization predictionMembrane StainingExperimental Organism SystemsGene TargetingArtifactsSequence AnalysisPlasmidsResearch ArticleProtein StructureSaccharomyces cerevisiae ProteinsBioinformaticsRecombinant Fusion ProteinsGenetic VectorsGreen Fluorescent ProteinsImmunologySaccharomyces cerevisiaeHemagglutinins ViralSaccharomyces cerevisiaeComputational biologyResearch and Analysis MethodsGreen Fluorescent ProteinGenomic InstabilityAntibodiesProtein–protein interactionProto-Oncogene Proteins c-mycSaccharomyces03 medical and health sciencesModel OrganismsAmino Acid Sequence AnalysisMolecular BiologyStaining and Labelinglcsh:ROrganismsFungiBiology and Life SciencesProteinsbiology.organism_classificationFusion proteinYeastLuminescent Proteins030104 developmental biologySpecimen Preparation and Treatmentlcsh:QProtein Structure NetworksPLOS ONE
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E2F1 interacts with BCL-xL and regulates its subcellular localization dynamics to trigger cell death

2018

International audience; E2F1 is the main pro-apoptotic effector of the pRB-regulated tumor suppressor pathway by promoting the transcription of various pro-apoptotic proteins. We report here that E2F1 partly localizes to mitochondria, where it favors mitochondrial outer membrane permeabilization. E2F1 interacts with BCL-xL independently from its BH3 binding interface and induces a stabilization of BCL-xL at mitochondrial membranes. This prevents efficient control of BCL-xL over its binding partners, in particular over BAK resulting in the induction of cell death. We thus identify a new, non-BH3-binding regulator of BCL-xL localization dynamics that influences its anti-apoptotic activity.

0301 basic medicineProgrammed cell deathTranscription Geneticbcl-X ProteinRegulatorBcl-xL[SDV.CAN]Life Sciences [q-bio]/CancerBCL-xL mobilityMitochondrionBiochemistrylaw.invention[ SDV.CAN ] Life Sciences [q-bio]/CancerE2F1 Subject Category Autophagy & Cell Death03 medical and health sciences[SDV.CAN] Life Sciences [q-bio]/CancerlawBCL-2 familyCell Line TumorGeneticsJournal ArticleHumansE2F1Molecular BiologyCell DeathbiologyManchester Cancer Research CentreEffectorChemistryResearchInstitutes_Networks_Beacons/mcrcScientific ReportsapoptosisSubcellular localizationMitochondriaCell biologyProtein Transportbcl-2 Homologous Antagonist-Killer Protein030104 developmental biologyGene Expression RegulationProto-Oncogene Proteins c-bcl-2biology.proteinSuppressorbiological phenomena cell phenomena and immunityExtracellular SpaceE2F1 Transcription FactorProtein Binding
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Diversity in AMPA receptor complexes in the brain.

2017

AMPA receptor (AMPAR) complexes comprise four of the AMPAR subunits GluA1-4 and several additional interacting proteins. Subunit composition determines AMPAR function. However, AMPAR function depends to a large extent also on interacting proteins, which influence trafficking to the cell surface, activity-dependent subcellular localization and gating of AMPARs. In this review we report about recent findings on the diversity of AMPAR complexes that allow us to better understand functional properties of native receptors in the brain.

0301 basic medicineProtein subunitCellGatingAMPA receptorBiology03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansReceptors AMPAReceptormusculoskeletal neural and ocular physiologyGeneral NeuroscienceBrainGenetic VariationSubcellular localizationTransport proteinProtein Transport030104 developmental biologymedicine.anatomical_structurenervous systemNeuroscience030217 neurology & neurosurgeryFunction (biology)Current opinion in neurobiology
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Visualizing Human Protein‐Protein Interactions and Subcellular Localizations on Cell Images Through CellMap

2020

Visualizing protein data remains a challenging and stimulating task. Useful and intuitive visualization tools may help advance biomolecular and medical research; unintuitive tools may bar important breakthroughs. This protocol describes two use cases for the CellMap (http://cellmap.protein.properties) web tool. The tool allows researchers to visualize human protein-protein interaction data constrained by protein subcellular localizations. In the simplest form, proteins are visualized on cell images that also show protein-protein interactions (PPIs) through lines (edges) connecting the proteins across the compartments. At a glance, this simultaneously highlights spatial constraints that prot…

0303 health sciencesgenetic structuresComputer scienceCells030305 genetics & heredityProteinsA proteinComputational biologyBiochemistryWeb toolProtein subcellular localization predictionVisualizationProtein–protein interaction03 medical and health sciencesImaging Three-DimensionalStructural BiologyProtein Interaction MappingHumansProtocol (object-oriented programming)SoftwareSubcellular Fractions030304 developmental biologyCurrent Protocols in Bioinformatics
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Different pathways for the nuclear import of yeast RNA polymerase II

2015

Recent studies suggest that RNA polymerase II (Pol II) has to be fully assembled before being imported into the nucleus, while other reports indicate a distinct mechanism to import large and small subunits. In yeast, Iwr1 binds to the holoenzyme assembled in the cytoplasm and directs its nuclear entry. However, as IWR1 is not an essential gene, Iwr1-independent pathway(s) for the nuclear import of Pol II must exist. In this paper, we investigate the transport into the nucleus of several large and small Pol II subunits in the mutants of genes involved in Pol II biogenesis. We also analyse subcellular localization in the presence of drugs that can potentially affect Pol II nuclear import. Our…

Active Transport Cell NucleusBiophysicsRNA polymerase IISaccharomyces cerevisiaeBiochemistrychemistry.chemical_compoundStructural BiologyRNA polymeraseGeneticsmedicineMolecular BiologyCell NucleusbiologyProcessivitySubcellular localizationMolecular biologyCell biologyCell nucleusmedicine.anatomical_structurechemistrybiology.proteinRNA Polymerase IITranscription factor II DNuclear transportCarrier ProteinsBiogenesisBiochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
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Cannabinoid control of brain bioenergetics: Exploring the subcellular localization of the CB1 receptor

2014

Brain mitochondrial activity is centrally involved in the central control of energy balance. When studying mitochondrial functions in the brain, however, discrepant results might be obtained, depending on the experimental approaches. For instance, immunostaining experiments and biochemical isolation of organelles expose investigators to risks of false positive and/or false negative results. As an example, the functional presence of cannabinoid type 1 (CB1) receptors on brain mitochondrial membranes (mtCB1) was recently reported and rapidly challenged, claiming that the original observation was likely due to artifact results. Here, we addressed this issue by directly comparing the procedures…

CB1 receptorWIN WIN55212-2Cannabinoid receptorBrain bioenergeticsLactate dehydrogenase Amedicine.medical_treatmentSDHADMSO dimethyl sulfoxideMitochondrionBiologySlp2 stomatin-like protein 2SDHA succinate dehydrogenase aTechnical ReportmedicineantibodieseducationReceptorKO knock-outMolecular Biologyeducation.field_of_studyelectron microscopyLDHa lactate dehydrogenase aDAB–Ni Ni-intensified 33ʹ-diaminobenzidine–4HClCell BiologySubcellular localizationWT wild-typemitochondriaBiochemistryCB1 cannabinoid type 1 receptorBSA bovine serum albuminCannabinoidorganelle purificationNeuroscienceImmunostainingMolecular Metabolism
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aPKCζ cortical loading is associated with Lgl cytoplasmic release and tumor growth in Drosophila and human epithelia

2007

Atypical protein kinase C (aPKC) and Lethal giant larvae (Lgl) regulate apical-basal polarity in Drosophila and mammalian epithelia. At the apical domain, aPKC phosphorylates and displaces Lgl that, in turn, maintains aPKC inactive at the basolateral region. The mutual exclusion of these two proteins seems to be crucial for the correct epithelial structure and function. Here we show that a cortical aPKC loading induces Lgl cytoplasmic release and massive overgrowth in Drosophila imaginal epithelia, whereas a cytoplasmic expression does not alter proliferation and epithelial overall structure. As two aPKC isoforms (iota and zeta) exist in humans and we previously showed that Drosophila Lgl i…

Cancer Researchmedicine.medical_specialtyCytoplasmAPKCz; Cell polarity; Drosophila; Hugl-1; Lethal giant larvae; Ovarian epithelial cancersAPKCzEpitheliumInternal medicineDrosophilidaeCell polarityGeneticsmedicineAnimalsDrosophila ProteinsHumansWings AnimalMolecular BiologyProtein kinase CProtein Kinase CCell ProliferationRegulation of gene expressionOvarian NeoplasmsbiologyTumor Suppressor ProteinsGene Expression Regulation DevelopmentalHugl-1Lethal giant larvaebiology.organism_classificationProtein subcellular localization predictionEpitheliumOvarian epithelial cancersCell biologyEndocrinologymedicine.anatomical_structureDrosophila melanogasterPhenotypeGene Expression RegulationCell polarityFemaleDrosophilaDrosophila melanogasterDrosophila Protein
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Lafora disease fibroblasts exemplify the molecular interdependence between thioredoxin 1 and the proteasome in mammalian cells

2013

13 páginas, 8 figuras (que no aparecen en este documento, se pueden consultar en: http://www.sciencedirect.com/science/article/pii/S0891584913003274#ec0005)

Cell signalingProteasome Endopeptidase ComplexBlotting WesternFree radicalsBiologyBiochemistryLafora diseaseThioredoxin 1MiceThioredoxinsPhysiology (medical)medicineAnimalsHumansImmunoprecipitationLafora diseaseEndoplasmic Reticulum Chaperone BiPCell proliferationMicroscopy ConfocalProteasomeReverse Transcriptase Polymerase Chain ReactionEndoplasmic reticulumCell cycleFibroblastsSubcellular localizationmedicine.diseaseFlow CytometryCell biologyRare diseasesCytosolOxidative StressBiochemistryProteasomeLafora DiseaseUnfolded protein responseNIH 3T3 CellsAntioxidant enzymesOxidation-Reduction
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Expression of protein kinase C gene family members is temporally and spatially regulated during neural development in vitro.

1998

We used primary cultures of rat hippocampal neurons and PCC7-Mz1 cells to correlate the expression of the protein kinase C (PKC) gene family with specific events during neural differentiation. Multipotent PCC7-Mz1 embryonic carcinoma stem cells develop into a tissue-like pattern of neuronal, fibroblast-like and astroglial cells by all-trans retinoic acid (RA) treatment. Western blot analyses demonstrate that PKCalpha, betaI, gamma, theta, mu, lambda, and zeta were constitutively expressed but the expression of PKCbetaII, delta, epsilon, and eta was up-regulated three days after addition of RA when cells mature morphologically. While the protein levels of the PKC isoforms betaII, delta and e…

Cell typeHistologyCellular differentiationBlotting WesternTretinoinBiologyGene Expression Regulation EnzymologicPathology and Forensic MedicineMiceTumor Cells CulturedAnimalsMARCKSProtein kinase CCells CulturedProtein Kinase CNeuronsNeurogenesisAntibodies MonoclonalCell DifferentiationCell BiologyGeneral MedicineSubcellular localizationMolecular biologyCell biologyRatsUp-RegulationIsoenzymesProtein BiosynthesisStem cellNeural developmentSubcellular FractionsEuropean journal of cell biology
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Subcellular localization of pentachlorophenol 4-monooxygenase in Sphingobium chlorophenolicum ATCC 39723.

2002

Abstract We have studied the subcellular localization of pentachlorophenol 4-monooxygenase (PCP4MO) in Sphingobium chlorophenolicum ATCC 39723 during induction by pentachlorophenol (PCP). Using a monoclonal antibody CL6 specific to the native and recombinant PCP4MO, the enzyme was primarily found soluble as determined by immunoblot and ELISA analyses of cellular fractions. However, the enzyme was observed both in the soluble and membrane-bound forms during induction for 2–4 h, suggesting its translocation out from the cytoplasm. Electron microscopy confirmed that PCP4MO was predominantly present in the cytoplasm at 1 h, whereas at 4 h significant amount was detected also in the membrane and…

CytoplasmBiophysicsBiologyProtein Sorting SignalsBiochemistryMixed Function Oxygenaseschemistry.chemical_compoundBiosynthesisAntibody SpecificityInner membraneMolecular BiologySphingobium chlorophenolicumAlphaproteobacteriachemistry.chemical_classificationAntibodies MonoclonalCell BiologyPeriplasmic spacebiology.organism_classificationSubcellular localizationMolecular biologyImmunohistochemistryPentachlorophenolKineticsEnzymechemistryBiochemistryCytoplasmPeriplasmBiochemical and biophysical research communications
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