Search results for "Coated vesicle"

showing 10 items of 26 documents

A Model for ERD2 Function in Higher Plants

2020

ER lumenal proteins have a K(H)DEL motif at their C-terminus. This is recognized by the ERD2 receptor (KDEL receptor in animals), which localizes to the Golgi apparatus and serves to capture escaped ER lumenal proteins. ERD2-ligand complexes are then transported back to the ER via COPI coated vesicles. The neutral pH of the ER causes the ligands to dissociate with the receptor being returned to the Golgi. According to this generally accepted scenario, ERD2 cycles between the ER and the Golgi, although it has been found to have a predominant Golgi localization. In this short article, we present a model for the functioning of ERD2 receptors in higher plants that explains why it is difficult t…

0106 biological sciences0301 basic medicineCOPI-Coated Vesiclescis-GolgiKDELMini ReviewPopulationPlant Sciencelcsh:Plant culture01 natural sciences03 medical and health sciencessymbols.namesakeERD2/KDEL receptorlcsh:SB1-1110Neutral phGolgi localizationeducationReceptorCOPII-vesicleeducation.field_of_studyChemistryGolgi apparatusCell biologysecretory unit030104 developmental biologyCOPI-vesiclesymbolsK(H)DEL ligandFunction (biology)010606 plant biology & botanyFrontiers in Plant Science
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Hepatitis B Virus Exploits ERGIC-53 in Conjunction with COPII to Exit Cells.

2020

Several decades after its discovery, the hepatitis B virus (HBV) still displays one of the most successful pathogens in human populations worldwide. The identification and characterization of interactions between cellular and pathogenic components are essential for the development of antiviral treatments. Due to its small-sized genome, HBV highly depends on cellular functions to produce and export progeny particles. Deploying biochemical-silencing methods and molecular interaction studies in HBV-expressing liver cells, we herein identified the cellular ERGIC-53, a high-mannose-specific lectin, and distinct components of the endoplasmic reticulum (ER) export machinery COPII as crucial factor…

0301 basic medicineHepatitis B virusSec24AEndosomeHBV assemblyVesicular Transport ProteinsN-glycosylationBiologymedicine.disease_causeEndoplasmic ReticulumTransfectionGenomeESCRTArticle03 medical and health sciencesN-linked glycosylationViral life cycleCell Line TumormedicineHBVHumansCOPIICOPIIlcsh:QH301-705.5Hepatitis B virus030102 biochemistry & molecular biologyEndosomal Sorting Complexes Required for TransportEndoplasmic reticulumVirionMembrane ProteinsGeneral MedicineHepatitis BHBV egressERGIC-53Cell biologyProtein Transport030104 developmental biologyMannose-Binding Lectinslcsh:Biology (General)HepatocytesLMAN-1COP-Coated VesiclesCells
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Shared midgut binding sites for Cry1A.105, Cry1Aa, Cry1Ab, Cry1Ac and Cry1Fa proteins from Bacillus thuringiensis in two important corn pests, Ostrin…

2013

First generation of insect-protected transgenic corn (Bt-corn) was based on the expression of Cry1Ab or Cry1Fa proteins. Currently, the trend is the combination of two or more genes expressing proteins that bind to different targets. In addition to broadening the spectrum of action, this strategy helps to delay the evolution of resistance in exposed insect populations. One of such examples is the combination of Cry1A.105 with Cry1Fa and Cry2Ab to control O. nubilalis and S. frugiperda. Cry1A.105 is a chimeric protein with domains I and II and the C-terminal half of the protein from Cry1Ac, and domain III almost identical to Cry1Fa. The aim of the present study was to determine whether the c…

Agricultural BiotechnologyApplied MicrobiologyCoated vesiclePlant SciencePlasma protein bindingMothsBiochemistryOstriniaPlagues ControlBacillus thuringiensisBiomacromolecule-Ligand InteractionsPlant PestsMultidisciplinaryMicrovillibiologyGenetically Modified OrganismsQRAgricultureRecombinant ProteinsBiochemistryLarvaMedicineDisease SusceptibilityAgrochemicalsResearch ArticleBiotechnologyProtein BindingScienceProtein domainBiotecnologia agrícolaBacillus thuringiensisCoated VesiclesCerealsCropsSpodopteraSpodopteraMicrobiologyBinding CompetitiveZea maysBacterial ProteinsBotanyAnimalsPesticidesBinding siteProtein InteractionsBiologyTransgenic PlantsfungiProteinsPlant Pathologybiology.organism_classificationFusion proteinMaizeGastrointestinal TractKineticsPlant BiotechnologyPest ControlProteïnes
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Clathrin-mediated constitutive endocytosis of PIN auxin efflux carriers in Arabidopsis.

2007

SummaryEndocytosis is an essential process by which eukaryotic cells internalize exogenous material or regulate signaling at the cell surface [1]. Different endocytic pathways are well established in yeast and animals; prominent among them is clathrin-dependent endocytosis [2, 3]. In plants, endocytosis is poorly defined, and no molecular mechanism for cargo internalization has been demonstrated so far [4, 5], although the internalization of receptor-ligand complexes at the plant plasma membrane has recently been shown [6]. Here we demonstrate by means of a green-to-red photoconvertible fluorescent reporter, EosFP [7], the constitutive endocytosis of PIN auxin efflux carriers [8] and their …

Auxin effluxmedia_common.quotation_subjectRecombinant Fusion ProteinseducationEndocytic cycleArabidopsisBiologyEndocytosisClathrinPlant RootsGeneral Biochemistry Genetics and Molecular BiologyExocytosisGenes ReporterPIN proteinsInternalizationmedia_commonAgricultural and Biological Sciences(all)Indoleacetic AcidsBiochemistry Genetics and Molecular Biology(all)Arabidopsis ProteinsProtoplastsCell MembraneClathrin-Coated VesiclesReceptor-mediated endocytosisClathrinEndocytosisCell biologyLuminescent Proteinsbiology.proteinCELLBIOGeneral Agricultural and Biological SciencesCurrent biology : CB
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Evidence for a selective and electroneutral K+/H+-exchange in Saccharomyces cerevisiae using plasma membrane vesicles

1996

The existence of a K+/H+ transport system in plasma membrane vesicles from Saccharomyces cerevisiae is demonstrated using fluorimetric monitoring of proton fluxes across vesicles (ACMA fluorescence quenching). Plasma membrane vesicles used for this study were obtained by a purification/reconstitution protocol based on differential and discontinuous sucrose gradient centrifugations followed by an octylglucoside dilution/gel filtration procedure. This method produces a high percentage of tightly-sealed inside-out plasma membrane vesicles. In these vesicles, the K+/H+ transport system, which is able to catalyse both K+ influx and efflux, is mainly driven by the K+ transmembrane gradient and ca…

Cell Membrane Permeability[SDV]Life Sciences [q-bio]Coated VesiclesCoated vesicleBiological Transport ActiveBioengineeringSaccharomyces cerevisiaeBiologyH(+)-K(+)-Exchanging ATPaseApplied Microbiology and BiotechnologyBiochemistryMembrane PotentialsCell membraneElectron Transport Complex IVH(+)-K(+)-Exchanging ATPasealpha-MannosidaseMannosidasesGeneticsmedicineCentrifugation Density GradientNa+/K+-ATPaseComputingMilieux_MISCELLANEOUSMembrane potentialVesicleCell MembraneDithiazanineElectron Transport Complex IVIsoxazolesHydrogen-Ion ConcentrationMembranemedicine.anatomical_structureSpectrometry Fluorescence[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryBiophysicsChromatography GelPotassiumProtonsMannoseBiotechnology
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Fabrication of polyelectrolyte multilayered vesicles as inhalable dry powder for lung administration of rifampicin

2014

A polyelectrolyte complex based on chitosan and carrageenan was used to coat rifampicin-loaded vesicles and obtain a dry powder for inhalation by spray-drying. The polymer complexation on vesicle surface stabilized them and improved their adhesion on airways and epithelia cells. Uncoated liposomes were small in size, negatively charged and able to incorporate large amounts of rifampicin (70%). Coated vesicles were still able to load adequate amounts of drug (∼70%) but the coating process produced larger particles (1 μm) that were positively charged and with a spherical shape. Aerosol performances, evaluated using the next-generation impactor, showed that coated vesicles reached the 50% of f…

Cell SurvivalDrug CompoundingPharmaceutical ScienceCoated vesicleCarrageenanChitosanchemistry.chemical_compoundX-Ray DiffractionCell Line TumorAdministration InhalationHumansParticle SizeAntibiotics Antitubercularchemistry.chemical_classificationChitosanLiposomeChromatographyCalorimetry Differential ScanningVesiclePolymerAdhesionPolyelectrolyteCarrageenanchemistryChemical engineeringLiposomesRifampinInternational Journal of Pharmaceutics
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Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.

2004

The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…

CoatPhysiologyAmino Acid MotifsArabidopsisReceptors Cytoplasmic and NuclearPlant ScienceBiologyCoat Protein Complex ICytosolAnimalsCOPIIBinding SitesVesicular-tubular clusterArabidopsis ProteinsCell BiologyGeneral MedicineCOPIPlant cellIn vitroPeptide FragmentsCell biologyRatsCytosolProtein TransportRat liverCOP-Coated VesiclesProtein BindingSignal TransductionPlantcell physiology
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ER-to-Golgi Transport: The COPII-Pathway

2006

The endoplasmic reticulum (ER) is the starting site of the journey of newly synthesized proteinsto the apoplast, plasma membrane and to the vacuolar compartments. Transport between these membranecompartments of the secretory pathway in eukaryotic cells is mediated by vesicles, which are producedby a budding mechanism involving coat proteins that capture specific cargo molecules and helppackage them into coated vesicles. These vesicles are known as COPII-coated vesicles, and are usuallyisolated after their induction in vitro using microsomal membranes, cytosol and a non-hydrolyzableGTP-analogue. COPII-coated vesicles are formed at specific sites in the ER known as ER-exit sites(ERES). ERES a…

Cytosolsymbols.namesakeChemistryEndoplasmic reticulumVesicleMicrosomesymbolsCoated vesicleGolgi apparatusCOPIISecretory pathwayCell biology
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Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate.

2007

Phosphatidylinositol 4,5-bisphosphate [PI(4,5) P 2 ], a phosphoinositide concentrated predominantly in the plasma membrane, binds endocytic clathrin adaptors, many of their accessory factors, and a variety of actin-regulatory proteins. Here we have used fluorescent fusion proteins and total internal reflection fluorescence microscopy to investigate the effect of acute PI(4,5) P 2 breakdown on the dynamics of endocytic clathrin-coated pit components and of the actin regulatory complex, Arp2/3. PI(4,5) P 2 breakdown was achieved by the inducible recruitment to the plasma membrane of an inositol 5-phosphatase module through the rapamycin/FRB/FKBP system or by treatment with ionomycin. PI(4,5)…

DynaminsPhosphatidylinositol 45-DiphosphateEpsinEndocytic cyclemacromolecular substancesEndocytosisClathrinClathrin coatModels Biologicalchemistry.chemical_compoundChlorocebus aethiopsAnimalsHumansDynaminSirolimusMultidisciplinarybiologyCell MembraneClathrin-Coated VesiclesBiological SciencesActinsEndocytosisCell biologyAdaptor Proteins Vesicular TransportPhosphatidylinositol 45-bisphosphatechemistryActin-Related Protein 3Actin-Related Protein 2COS Cellsbiology.proteinLamellipodiumProceedings of the National Academy of Sciences of the United States of America
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Hepatitis B subviral envelope particles use the COPII machinery for intracellular transport via selective exploitation of Sec24A and Sec23B

2020

Hepatitis B virus (HBV) is a leading cause of liver disease. Its success as a human pathogen is related to the immense production of subviral envelope particles (SVPs) contributing to viral persistence by interfering with immune functions. To explore cellular pathways involved in SVP formation and egress, we investigated host-pathogen interactions. Yeast-based proteomics revealed Sec24A, a component of the coat protein complex II (COPII), as an interaction partner of the HBV envelope S domain. To understand how HBV co-opts COPII as a proviral machinery, we studied roles of key Sec proteins in HBV-expressing liver cells. Silencing of Sar1, Sec23, and Sec24, which promote COPII assembly conco…

Hepatitis B virusImmunology610 MedizinVesicular Transport ProteinsBiologymedicine.disease_causeProteomicsEndoplasmic ReticulumMicrobiologyCell Line03 medical and health sciencesDownregulation and upregulationTranscription (biology)610 Medical sciencesVirologyddc:570medicineGene silencingHumansProtein IsoformsSecretionRNA Small InterferingCOPII030304 developmental biologyHepatitis B virus0303 health sciences030306 microbiologyEndoplasmic reticulumBiological TransportHepatitis Bdiseases infection microbe–cell interaction proteomics virusesCell biologyHost-Pathogen InteractionsHepatocytesCOP-Coated Vesicles
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