Search results for "Subcellular localization"

showing 10 items of 53 documents

The budding yeast Start repressor Whi7 differs in regulation from Whi5, emerging as a major cell cycle brake in response to stress

2020

ABSTRACT Start is the main decision point in the eukaryotic cell cycle at which cells commit to a new round of cell division. It involves the irreversible activation of a transcriptional programme through the inactivation of Start transcriptional repressors: the retinoblastoma family in mammals, or Whi5 and its recently identified paralogue Whi7 (also known as Srl3) in budding yeast. Here, we provide a comprehensive comparison of Whi5 and Whi7 that reveals significant qualitative differences. Indeed, the expression, subcellular localization and functionality of Whi7 and Whi5 are differentially regulated. Importantly, Whi7 shows specific properties in its association with promoters not share…

Saccharomyces cerevisiae ProteinsCell division[SDV]Life Sciences [q-bio]RepressorSaccharomyces cerevisiaeBiologyCell cycleCicle cel·lularStress13503 medical and health sciences0302 clinical medicineWhi7Gene Expression Regulation FungalmedicineWhi5030304 developmental biology0303 health sciencesRetinoblastomaCèl·lules eucariotesPromoterCell BiologyCell cycleSubcellular localizationmedicine.diseaseStartBudding yeastCell biologyRepressor ProteinsDecision points[SDV] Life Sciences [q-bio]SaccharomycetalesCell Division030217 neurology & neurosurgeryResearch Article
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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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GFP immunogold staining, from light to electron microscopy, in mammalian cells.

2012

GFP has emerged as an important reporter for monitoring gene expression, protein localization, cell transformation and cell lineage. The development of GFP as a marker in many different biological systems has emphasized the need to image GFP at high resolution. GFP immunogold labeling with colloidal gold particles becomes essential for electron microscopy (EM) ultrastructural detection. Because of the small size, colloidal gold particles require silver enhancement, a procedure to increase the size of the particle as well as gold toning to stabilize the silver layer. GFP preembedding immunogold staining enables high quality cellular-ultrastructural EM analysis mainly for two reasons, on one …

Staining and LabelingGreen Fluorescent ProteinsGeneral Physics and AstronomyHigh resolutionCell BiologyImmunogold labellingCell lineageBiologyProtein subcellular localization predictionMolecular biologyImmunohistochemistrylaw.inventionGreen fluorescent proteinStructural BiologylawColloidal goldBiophysicsUltrastructureAnimalsHumansGeneral Materials ScienceElectron microscopeFluorescent DyesMicron (Oxford, England : 1993)
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Expression of solute carrier 7A4 (SLC7A4) in the plasma membrane is not sufficient to mediate amino acid transport activity.

2002

Member 4 of human solute carrier family 7 (SLC7A4) exhibits significant sequence homology with the SLC7 subfamily of human cationic amino acid transporters (hCATs) [Sperandeo, Borsani, Incerti, Zollo, Rossi, Zuffardi, Castaldo, Taglialatela, Andria and Sebastio (1998) Genomics 49, 230–236]. It is therefore often referred to as hCAT-4 even though no convincing transport activity has been shown for this protein. We expressed SLC7A4 in Xenopus laevis oocytes, but could not detect any transport activity for cationic, neutral or anionic amino acids or for the polyamine putrescine. In addition, human glioblastoma cells stably overexpressing a fusion protein between SLC7A4 and the enhanced green f…

TeratocarcinomaAmino Acid Transport System y+Recombinant Fusion ProteinsGreen Fluorescent ProteinsMolecular Sequence DataRetinoic acidBiologyArginineBiochemistryPolymerase Chain ReactionGreen fluorescent proteinchemistry.chemical_compoundXenopus laevisTumor Cells CulturedAnimalsHumansAmino acid transporterAmino Acid SequenceAmino AcidsMolecular BiologyPeptide sequenceDNA Primerschemistry.chemical_classificationMammalsSequence Homology Amino AcidCell MembraneCell BiologySubcellular localizationFusion proteinAmino acidSolute carrier familyKineticsLuminescent ProteinschemistryBiochemistryGlioblastomaSequence AlignmentResearch Article
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Yeast karyopherin Kap95 is required for cell cycle progression at Start

2010

Abstract Background The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. Results When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel r…

Transcriptional ActivationSaccharomyces cerevisiae ProteinsNuclear Localization SignalsActive Transport Cell NucleusSaccharomyces cerevisiaeImportinBiologylcsh:QH573-671Transcription factorCells CulturedKaryopherinCell Nucleuschemistry.chemical_classificationlcsh:CytologyCell CycleCell BiologyCell cyclebeta KaryopherinsSubcellular localizationCell biologyDNA-Binding ProteinschemistryCytoplasmMutationTranscription Initiation SiteNuclear transportNuclear localization sequenceProtein BindingTranscription FactorsResearch ArticleBMC Cell Biology
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Increased AICD generation does not result in increased nuclear translocation or activation of target gene transcription.

2008

A sequence of amyloid precursor protein (APP) cleavages culminates in the sequential release of the APP intracellular domain (AICD) and the amyloid beta peptide (Abeta) and/or p3 fragment. One of the environmental factors favouring the accumulation of AICD appears to be a rise in intracellular pH. Here we further identified the metabolism and subcellular localization of artificially expressed constructs under such conditions. We also co-examined the mechanistic lead up to the AICD accumulation and explored possible significances for its increased expression. We found that most of the AICD generated under pH neutralized conditions is likely cleaved from C83. While the AICD surplus was unable…

Transcriptional ActivationTranscription GeneticAmyloid betaActive Transport Cell NucleusCHO CellsModels BiologicalTransactivationAmyloid beta-Protein PrecursorCricetulusTranscription (biology)CricetinaeAmyloid precursor proteinAnimalsHumansLuciferaseCells CulturedRegulation of gene expressionCell NucleusbiologyCell BiologyHydrogen-Ion ConcentrationSubcellular localizationMolecular biologyCell biologyProtein Structure TertiaryCytosolbiology.proteinProtein Processing Post-TranslationalProtein BindingExperimental cell research
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Cellular and Subcellular Localization of Peroxidase Isoenzymes in Plants and Cell Suspension Cultures from Lupinus polyphyllus

1989

Abstract , leaf protoplasts and cell suspension cultures of Lupinus polyphyllus and isolated vacuoles were studied for cellular and subcellular localization of peroxidase isoenzymes. Isoelectric focusing revealed 16 peroxidase isoenzymes. The basic peroxidase isoenzymes are predominantly localized in the vacuole and, to a minor degree, unbound in the intercellular space. The acidic isoenzymes are cell wall-bound in plants and not detectable in suspension-cultured cells. Large amounts (up to 11.0 U/ml) of a single basic isoenzyme are detectable in the spent medium of cell suspension cultures.

biologyChemistryLupinus polyphyllusIsoelectric focusingCellVacuoleProtoplastSubcellular localizationbiology.organism_classificationMolecular biologyIsozymeGeneral Biochemistry Genetics and Molecular Biologymedicine.anatomical_structureBiochemistrybiology.proteinmedicinePeroxidaseZeitschrift für Naturforschung C
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Subcellular distribution of calpain-1 and calpain-2 as a key event for calpain-mediated functions in physiological and neoplastic mammary models

2019

Calpains are a family of calcium-dependent proteases, which modulate their substrates rather than degrade them in such a way that modifies them. Calpains deregulations have been determined as an aggravating factor of different diseases, including cancer. Nevertheless, there are no clear records about the particular contribution of each calpain isoform in physiological processes and how these isoforms are deregulated in pathological conditions. In vivo, each calpain isoform recognizes specific proteins as substrates, and it has been suggested that calpains subcellular localization might determine their substrate recognition, and consequently their functions. In the present study we have expl…

breast cancer:CIENCIAS DE LA VIDA::Biología celular [UNESCO]calpain-2UNESCO::CIENCIAS MÉDICASUNESCO::CIENCIAS TECNOLÓGICAS::Tecnología bioquímicacalpain subcellular localizationUNESCO::CIENCIAS DE LA VIDA::Biología celularcalpain-1mammary gland involution:CIENCIAS MÉDICAS [UNESCO]:CIENCIAS TECNOLÓGICAS::Tecnología bioquímica [UNESCO]
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Functional interactions between members of the REPAT family of insect pathogen-induced proteins

2012

Studies on the transcriptional response to pathogens in the insect larval gut have shown the regulation of several genes after the infection. Repat (REsponse to PAThogens) genes were first identified in Spodoptera exigua midgut as being up-regulated in response to the exposure to Bacillus thuringiensis toxins and baculovirus. Recently, new members of the REPAT family showed a constitutive up-regulation in a B. thuringiensis-resistant population. Based on a yeast two-hybrid screening, we have detected the interaction of REPAT1 with other members of the REPAT family, leading to the discovery of a new member: REPAT8. The functional role of this interaction was shown by following the changes of…

education.field_of_studybiologyPopulationMidgutSpodopteraSubcellular localizationbiology.organism_classificationmedicine.disease_causeMicrobiologyInsect ScienceBacillus thuringiensisGeneticsmedicineeducationMolecular BiologyGenePathogenEscherichia coliInsect Molecular Biology
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AMPA Receptor Auxiliary Proteins of the CKAMP Family

2019

α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors are assembled of four core subunits and several additional interacting proteins. Cystine-knot AMPA receptor-modulating proteins (CKAMPs) constitute a family of four proteins that influence the trafficking, subcellular localization and function of AMPA receptors. The four CKAMP family members CKAMP39/shisa8, CKAMP44/shisa9, CKAMP52/shisa6 and CKAMP59/shisa7 differ in their expression profile and their modulatory influence on AMPA receptor function. In this review, I report about recent findings on the differential roles of CKAMP family members.

glutamate receptorhippocampusGene ExpressionReviewAMPA receptorBiologySynaptic TransmissionCatalysisCell Linelcsh:ChemistryInorganic ChemistryLong term plasticitylateral geniculate nucleusAnimalsHumansAmino Acid SequenceReceptors AMPAAMPA receptorPhysical and Theoretical Chemistrysynaptic functionReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyNeuronal Plasticitymusculoskeletal neural and ocular physiologyOrganic ChemistryGlutamate receptorGeniculate BodiesGeneral MedicineSubcellular localizationlong-term plasticityComputer Science ApplicationsCell biologyProtein TransportSynaptic functionlcsh:Biology (General)lcsh:QD1-999nervous systemauxiliary subunitMultigene FamilySynapsesCarrier ProteinsIon Channel Gatingshort-term plasticityFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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