Search results for "sorting signals"

showing 10 items of 24 documents

Sorting Motifs Involved in the Trafficking and Localization of the PIN1 Auxin Efflux Carrier

2016

In contrast with the wealth of recent reports about the function of μ-adaptins and clathrin adaptor protein (AP) complexes, there is very little information about the motifs that determine the sorting of membrane proteins within clathrin-coated vesicles in plants. Here, we investigated putative sorting signals in the large cytosolic loop of the Arabidopsis (Arabidopsis thaliana) PIN-FORMED1 (PIN1) auxin transporter, which are involved in binding μ-adaptins and thus in PIN1 trafficking and localization. We found that Phe-165 and Tyr-280, Tyr-328, and Tyr-394 are involved in the binding of different μ-adaptins in vitro. However, only Phe-165, which binds μA(μ2)- and μD(μ3)-adaptin, was found …

0106 biological sciences0301 basic medicinePhysiologyPhenylalanineGreen Fluorescent ProteinsMutantArabidopsisPlant ScienceProtein Sorting SignalsEndoplasmic ReticulumEndocytosis01 natural sciencesClathrin03 medical and health sciencesCytosolGeneticsGuanine Nucleotide Exchange FactorsSecretory pathwaybiologyArabidopsis ProteinsEndoplasmic reticulumMembrane Transport ProteinsSignal transducing adaptor proteinArticlesPlants Genetically ModifiedClathrinEndocytosisAdaptor Protein Complex mu SubunitsTransport proteinCell biologyProtein Transport030104 developmental biologyProtein Sorting SignalsMutationbiology.protein010606 plant biology & botanyPlant Physiology
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Enhancing heterologous protein expression and secretion in HEK293 cells by means of combination of CMV promoter and IFNα2 signal peptide

2016

Efficient production and secretion of recombinant proteins in mammalian cell lines relies in a combination of genetic, metabolic and culture strategy factors. The present work assesses the influence of two key genetic components of expression vectors (promoter and signal peptide) on protein production and secretion effciency in HEK293 cells expressing eGFP as a reporter protein. Firstly, the strength of 3 different promoters was evaluated using transient expression methods. Flow cytometry analysis revealed that the highest level of intracellular protein expression was found when eGFP was under the control of CMV promoter, being 3-times higher in comparison to the rest of the promoters teste…

0106 biological sciences0301 basic medicineSignal peptideGreen Fluorescent ProteinsCytomegalovirusHeterologousBioengineeringProtein Sorting SignalsBiology01 natural sciencesApplied Microbiology and BiotechnologyGreen fluorescent protein03 medical and health sciences010608 biotechnologyProtein biosynthesisHumansSecretionPromoter Regions GeneticExpression vectorInterferon-alphaPromoterGeneral MedicineMolecular biologyRecombinant ProteinsHEK293 Cells030104 developmental biologyCell cultureBiotechnologyJournal of Biotechnology
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Increased antigen presentation efficiency by coupling antigens to MHC class I trafficking signals.

2007

Abstract Genetic modification of vaccines by linking the Ag to lysosomal or endosomal targeting signals has been used to route Ags into MHC class II processing compartments for improvement of CD4+ T cell responses. We report in this study that combining an N-terminal leader peptide with an MHC class I trafficking signal (MITD) attached to the C terminus of the Ag strongly improves the presentation of MHC class I and class II epitopes in human and murine dendritic cells (DCs). Such chimeric fusion proteins display a maturation state-dependent subcellular distribution pattern in immature and mature DCs, mimicking the dynamic trafficking properties of MHC molecules. T cell response analysis in…

CD4-Positive T-LymphocytesT cellRecombinant Fusion ProteinsImmunologyAntigen presentationMolecular Sequence DataMice Inbred StrainsCD8-Positive T-LymphocytesProtein Sorting SignalsMajor histocompatibility complexTransfectionViral Matrix ProteinsEpitopesMiceAntigens NeoplasmMHC class ImedicineImmunology and AllergyAnimalsHumansAmino Acid SequenceAntigensMHC class IIAntigen PresentationbiologyAntigen processingHistocompatibility Antigens Class IVaccinationMembrane ProteinsDendritic CellsMHC restrictionPhosphoproteinsCell biologyProtein Transportmedicine.anatomical_structurebiology.proteinCD8Journal of immunology (Baltimore, Md. : 1950)
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Protein targeting to the plasma membrane of adult skeletal muscle fiber: an organized mosaic of functional domains.

2001

The plasma membrane of differentiated skeletal muscle fibers comprises the sarcolemma, the transverse (T) tubule network, and the neuromuscular and muscle-tendon junctions. We analyzed the organization of these domains in relation to defined surface markers, beta-dystroglycan, dystrophin, and caveolin-3. These markers were shown to exhibit highly organized arrays along the length of the fiber. Caveolin-3 and beta-dystroglycan/dystrophin showed distinct, but to some extent overlapping, labeling patterns and both markers left transverse tubule openings clear. This labeling pattern revealed microdomains over the entire plasma membrane with the exception of the neuromuscular and muscle-tendon j…

Caveolin 3Muscle Fibers SkeletalNeuromuscular JunctionMuscle ProteinsProtein Sorting Signalsmedicine.disease_causeCaveolinsT-tubuleDystrophinMiceMembrane MicrodomainsViral Envelope ProteinsProtein targetingmedicineMyocyteAnimalsDystroglycansMuscle SkeletalGlycoproteinsSarcolemmaMembrane GlycoproteinsbiologyCell MembraneSkeletal muscleCell BiologyMolecular biologyTransport proteinCell biologyRatsCytoskeletal ProteinsProtein Transportmedicine.anatomical_structureTubulebiology.proteinFemaleDystrophinExperimental cell research
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The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression

2008

Inner nuclear membrane proteins containing a LEM (LAP2, emerin, and MAN1) domain participate in different processes, including chromatin organization, gene expression, and nuclear envelope biogenesis. In this study, we identify a robust genetic interaction between transcription export (TREX) factors and yeast Src1, an integral inner nuclear membrane protein that is homologous to vertebrate LEM2. DNA macroarray analysis revealed that the expression of the phosphate-regulated genes PHO11, PHO12, and PHO84 is up-regulated in src1Δ cells. Notably, these PHO genes are located in subtelomeric regions of chromatin and exhibit a perinuclear location in vivo. Src1 spans the nuclear membrane twice an…

Chromatin ImmunoprecipitationSaccharomyces cerevisiae ProteinsGenes FungalSaccharomyces cerevisiaeProtein Sorting SignalsBiologyArticleGenètica molecularProton-Phosphate SymportersGene Expression Regulation FungalGene expressionmedicineExpressió genèticaInner membraneNuclear proteinNuclear poreNuclear membraneResearch ArticlesNucleoplasmMembrane ProteinsNuclear ProteinsCell BiologyTelomereMolecular biologyChromatinProtein Structure TertiaryChromatinAlternative SplicingGenòmicamedicine.anatomical_structureMultiprotein ComplexesNuclear lamina
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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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Primary Structure of Selected Archaeal Mesophilic and Extremely Thermophilic Outer Surface Layer Proteins

2002

The archaea are recognized as a separate third domain of life together with the bacteria and eucarya. The archaea include the methanogens, extreme halophiles, thermoplasmas, Sulfate reducers and Sulfur metabolizing thermophiles, which thrive in different habitats such as anaerobic niches, salt lakes, and marine hydrothermals systems and continental solfataras. Many of these habitats represent extreme environments in respect to temperature, osmotic pressure and pH-values and remind on the conditions of the early earth. The cell envelope structures were one of the first biochemical characteristics of archaea studied in detail. The most common archaeal cell envelope is composed of a single cry…

Hot TemperaturebiologyArchaeal ProteinsThermophileThermoplasmaMembrane ProteinsProtein Sorting Signalsbiology.organism_classificationArchaeaApplied Microbiology and BiotechnologyMicrobiologyProtein Structure SecondaryHalophileBiochemistryExtreme environmentAmino Acid SequenceAmino AcidsCell envelopeProtein stabilizationSequence AlignmentS-layerEcosystemEcology Evolution Behavior and SystematicsArchaeaSystematic and Applied Microbiology
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An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase

1991

AbstractTo gain an understanding of the mechanism by which the subcellular distribution of cytosolic epoxide hydrolase (cEH) is directed, we have analyzed the carboxy terminal region of rat liver cEH by means of cDNA cloning to define the structure of its possible peroxisomal targeting sequence (PTS). Purified cEH was subjected to peptide analysis following endoproteinase Glu-C digestion and HPLC-separation of the fragments. The obtained sequence information was used to perform PCR experiments resulting in the isolation of a 680 bp cDNA clone encoding the carboxy terminus of cEH. The deduced amino acid sequence displays a terminal tripeptide Ser-Lys-Ile which is highly homologous to the PTS…

MaleSignal peptidePTSanimal structures1303 BiochemistryMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthTripeptideProtein Sorting SignalsBiologyMicrobodiesBiochemistryAmino acid sequence1307 Cell BiologyCytosol1315 Structural Biology1311 GeneticsStructural BiologyComplementary DNAGenetics1312 Molecular BiologyAnimalsCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceEpoxide Hydrolaseschemistry.chemical_classificationBase SequencecDNA sequenceDNACell BiologyPeroxisomeMolecular biologyRatsIsoenzymesCytosolPCREnzymeLiverchemistryBiochemistrycEH570 Life sciences; biologyPeptide analysis1304 Biophysics
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A novel transmembrane domain mediating retention of a highly motile herpesvirus glycoprotein in the endoplasmic reticulum

2010

Gene m164 of murine cytomegalovirus belongs to the large group of 'private' genes that show no homology to those of other cytomegalovirus species and are thought to represent 'host adaptation' genes involved in virus-host interaction. Previous interest in the m164 gene product was based on the presence of an immunodominant CD8 T-cell epitope presented at the surface of infected cells, despite interference by viral immune-evasion proteins. Here, we provide data to reveal that the m164 gene product shows unusual features in its cell biology. A novel strategy of mass-spectrometric analysis was employed to map the N terminus of the mature protein, 107 aa downstream of the start site of the pred…

MuromegalovirusKKXXEndoplasmic reticulumMembrane ProteinsER retentionSTIM1Protein Sorting SignalsBiologyEndoplasmic ReticulumMass SpectrometryTransmembrane proteinCell biologyTransport proteinMolecular WeightGene productOpen Reading FramesProtein TransportViral ProteinsTransmembrane domainBiochemistryVirologyCOS CellsChlorocebus aethiopsAnimalsGlycoproteinsJournal of General Virology
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Features of TAP-independent MHC class I ligands revealed by quantitative mass spectrometry.

2008

TAP is responsible for transferring cytosolic peptides into the ER, where they can be loaded onto MHC molecules. Deletion of TAP results in a drastic reduction of MHC class I surface expression and alters the presented peptide pattern. This key molecule in antigen processing is tackled by several viruses and lost in some tumors, rendering the altered cells less vulnerable to T cell-based immune surveillance. Using the TAP-deficient cell line LCL721.174 and its TAP-expressing progenitor cell line LCL721.45, we identified and quantified more than 160 HLA ligands, 50 of which were presented TAP-independently. Peptides which were predominantly presented on the TAP-deficient LCL721.174 cell line…

Proteasome Endopeptidase ComplexImmunologyAntigen presentationEpitopes T-LymphocyteGene ExpressionHuman leukocyte antigenCysteine Proteinase InhibitorsProtein Sorting SignalsMajor histocompatibility complexCell LineAntigenATP Binding Cassette Transporter Subfamily B Member 3HLA AntigensTandem Mass SpectrometryMHC class IHLA-A2 AntigenImmunology and AllergyHumansAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Antigen PresentationbiologyHLA-A AntigensAntigen processingHistocompatibility Antigens Class IProteinsTransporter associated with antigen processingMHC restrictionMolecular biologyPeptide FragmentsCell biologyHLA-B AntigensIsotope Labelingbiology.proteinATP-Binding Cassette TransportersProteasome InhibitorsGene DeletionProtein BindingEuropean journal of immunology
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