Search results for "Golgi"

showing 10 items of 97 documents

Putative p24 complexes in Arabidopsis contain members of the delta and beta subfamilies and cycle in the early secretory pathway

2013

p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies, the latter probably including two different subclasses. It has previously been shown that transiently expressed red fluorescent protein (RFP)-p24δ5 (p24δ1 subclass) localizes to the endoplasmic reticulum (ER) at steady state as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. It is now shown that tr…

PhysiologyArabidopsisGolgi ApparatusPlant ScienceEndoplasmic ReticulumGreen fluorescent proteinsymbols.namesakeArabidopsisImmunoprecipitationER–Golgi transportcoat protein II (COPII)Secretory pathwayMicroscopy ConfocalSecretory PathwaybiologyArabidopsis ProteinsEndoplasmic reticulumcoat protein I (COPI)COPIImmunogold labellingGolgi apparatussecretory pathway.biology.organism_classificationImmunohistochemistryCell biologyMicroscopy Electronp24 proteinsMembrane proteinsymbolsResearch PaperPlasmidsJournal of Experimental Botany
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Coupled transport of Arabidopsis p24 proteins at the ER–Golgi interface

2012

p24 proteins are a family of type I membrane proteins localized to compartments of the early secretory pathway and to coat protein I (COPI)- and COPII-coated vesicles. They can be classified, by sequence homology, into four subfamilies, named p24α, p24β, p24γ, and p24δ. In contrast to animals and fungi, plants contain only members of the p24β and p24δ subfamilies. It has previously been shown that transiently expressed red fluorescent protein (RFP)–p24δ5 localizes to the endoplasmic reticulum (ER) as a consequence of highly efficient COPI-based recycling from the Golgi apparatus. Using specific antibodies, endogenous p24δ5 has now been localized to the ER and p24β2 to the Golgi apparatus in…

PhysiologyMolecular Sequence DataArabidopsisGolgi ApparatusPlant ScienceBiologyEndoplasmic Reticulumcoat protein (COP) IIcoat protein (COP) Isymbols.namesakeAmino Acid SequenceER–Golgi transportCOPIISecretory pathwayArabidopsis ProteinsVesicular-tubular clusterEndoplasmic reticulumMembrane ProteinsCOPIGolgi apparatussecretory pathwayTransport proteinCell biologyProtein TransportSecretory proteinp24 proteinssymbolsProtein BindingResearch PaperJournal of Experimental Botany
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Entry of Human Parechovirus 1

2001

ABSTRACT Human parechovirus 1 (HPEV-1) is a prototype member of parechoviruses, a recently established picornavirus genus. Although there is preliminary evidence that HPEV-1 recognizes α V integrins as cellular receptors, our understanding of early events during HPEV-1 infection is still very limited. The aim of this study was to clarify the entry mechanisms of HPEV-1, including the attachment of the virus onto the host cell surface and subsequent internalization. In blocking experiments with monoclonal antibodies against different receptor candidates, antibodies against α V and β 3 integrin subunits, in particular in combination, appeared to be the most efficient ones in preventing the HPE…

PicornavirusEndosomeImmunologyEndocytic cycleGolgi ApparatusHuman parechovirus 1EndosomesPicornaviridaePlatelet Membrane GlycoproteinsEndoplasmic ReticulumVirus ReplicationCaveolinsMicrobiologyClathrinEEA103 medical and health sciencessymbols.namesakeCapsidAntigens CDVirologyTumor Cells CulturedHumans030304 developmental biologyHost cell surface0303 health sciencesbiology030302 biochemistry & molecular biologyIntegrin beta3Clathrin-Coated VesiclesIntegrin alphaVGolgi apparatusbiology.organism_classificationVirologyClathrinEndocytosisVirus-Cell Interactions3. Good healthCell biologyInsect Sciencesymbolsbiology.proteinReceptors VirusJournal of Virology
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Out for a Walk Along the Secretory Pathway During Programmed Cell Death

2015

This chapter provides a comprehensive updated analysis on the role of the secretory pathway in the orchestration of cell’s demise, an emerging and promising research topic in the field of plant programmed cell death (PCD). Since my first review on this topic, a plethora of data has been published supporting the concept that endomembrane system-forming subcellular compartments cooperate to coordinate cellular responses to developmental and environmental cues and thereby can dictate a cell’s ultimate fate. Thus, the early secretory pathway, encompassing the endoplasmic reticulum and Golgi apparatus, can be involved in the perception of extrinsic and intrinsic stimuli. It can also be an active…

Programmed cell deathEndoplasmic reticulumfungifood and beveragesVacuoleBiologyGolgi apparatusCell biologysymbols.namesakeOrganellesymbolsCompartment (development)Endomembrane systemSecretory pathway
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Death of mitochondria during programmed cell death of leaf mesophyll cells

2005

The role of plant mitochondria in the programmed cell death (PCD) is widely discussed. However, spectrum and sequence of mitochondrial structural changes during different types of PCD in leaves are poorly described. Pea, cucumber and rye plants were grown under controlled growing conditions. A part of them were sprinkled with ethylene releaser to accelerate cell death. During yellowing the palisade parenchyma mitochondria were attracted to nuclear envelope. Mitochondrial matrix became electron translucent. Mitochondria entered vacuole by invagination of tonoplast and formed multivesicular bodies. Ethephon treatment increased the frequency of sticking of mitochondria to the nuclear envelope …

Programmed cell deathfood and beveragesApoptosisCell BiologyGeneral MedicineVacuoleMitochondrionPeroxisomeGolgi apparatusBiologyMitochondriaCell biologyPlant LeavesChloroplastsymbols.namesakeOrganophosphorus CompoundsPlant Growth RegulatorsApoptosissymbolsUltrastructurePlant Physiological PhenomenaCell Biology International
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The N-glycan processing in HT-29 cells is a function of their state of enterocytic differentiation. Evidence for an atypical traffic associated with …

1991

International audience; When the human colon cancer cells HT-29 undergo enterocytic differentiation, they correctly process their N-glycans, whereas their undifferentiated counterpart are unable to process Man9-8-GlcNAc2 species, the natural substrate of alpha-mannosidase I. As this enzyme is fully active in both HT-29 cell populations, we hypothesize that N-glycoproteins are unable to reach the cis Golgi, the site where alpha-mannosidase I has been localized. We have demonstrated this point by using 1-deoxymannojirimycin, leupeptin, and monensin. In the presence of 1-deoxymannojirimycin, a specific inhibitor of alpha-mannosidase I, differentiated HT-29 cells, as expected, accumulate Man9-8…

Proteases1-DeoxynojirimycinColonLeupeptinsCellular differentiationCellIn Vitro TechniquesBiologyBiochemistry03 medical and health sciencessymbols.namesakechemistry.chemical_compoundPolysaccharidesalpha-Mannosidase[ CHIM.ORGA ] Chemical Sciences/Organic chemistryMannosidasesTumor Cells CulturedmedicineHumansMonensinMolecular Biology030304 developmental biologychemistry.chemical_classificationGlucosamine0303 health sciencesMembrane Glycoproteins[CHIM.ORGA]Chemical Sciences/Organic chemistryEndoplasmic reticulum030302 biochemistry & molecular biologyLeupeptinBiological TransportCell DifferentiationCell BiologyCompartment (chemistry)Golgi apparatus[CHIM.ORGA] Chemical Sciences/Organic chemistrymedicine.anatomical_structureBiochemistrychemistryColonic NeoplasmssymbolsGlycoproteinProtein Processing Post-Translational
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Missense mutations of dual oxidase 2 (DUOX2) implicated in congenital hypothyroidism have impaired trafficking in cells reconstituted with DUOX2 matu…

2007

Abstract Dual oxidase 2 (DUOX2), a reduced NAD phosphate:O2 oxidoreductase flavoprotein, is a component of the thyrocyte H2O2 generator required for hormone synthesis at the apical plasma membrane. We recently identified a specific DUOX2 maturation factor (DUOXA2) that is necessary and sufficient for expression of functional DUOX2 in mammalian cell lines. We have now used a DUOXA2 reconstituted system to provide the first characterization of natural DUOX2 missense variants (Q36H, R376W, D506N) at the molecular level, analyzing their impact on H2O2 generation, trafficking, stability, folding, and DUOXA2 interaction. The Q36H and R376W mutations completely prevent routing of DUOX2 to the cell…

Protein FoldingMutantMutation MissenseBiologyEndoplasmic ReticulumCell membranesymbols.namesakeEndocrinologyMutant proteinPolysaccharidesCalnexinmedicineCongenital HypothyroidismAnimalsHumansMolecular BiologyCells CulturedFlavoproteinsOxidative foldingEndoplasmic reticulumCell MembraneMembrane ProteinsNADPH OxidasesDual oxidase 2General MedicineHydrogen PeroxideGolgi apparatusDual OxidasesRatsProtein Transportmedicine.anatomical_structureMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseBiochemistrysymbolsOxidation-ReductionMolecular endocrinology (Baltimore, Md.)
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Dithiothreitol Treatment of Madin-Darby Canine Kidney Cells Reversibly Blocks Export from the Endoplasmic Reticulum but Does Not Affect Vectorial Tar…

1995

Addition of dithiothreitol (DTT) to the culture medium of Madin-Darby canine kidney (MDCK) cells blocks transport of newly synthesized gp80 (clusterin, apolipoprotein J), a soluble marker protein for apical exocytosis in this epithelial cell line. In cells treated with DTT during pulse labeling, gp80 is retained in the endoplasmic reticulum. After removal of the reducing agent, gp80 is posttranslationally oxidized and secreted at the apical surface of MDCK cell monolayers. This demonstrates that when folded and oxidized posttranslationally, gp80 can acquire a conformation that exhibits sorting signals for vectorial targeting. In the continuous presence of DTT, the transepithelial electrical…

Protein FoldingProtein ConformationBiologyEndoplasmic ReticulumKidneySulfur RadioisotopesBiochemistryEpitheliumExocytosisDithiothreitolCell LineMembrane Potentialssymbols.namesakechemistry.chemical_compoundDogsMethioninemedicineAnimalsCysteineSalivary Proteins and PeptidesMolecular BiologySecretory pathwayGlycoproteinsTight junctionEndoplasmic reticulumCell MembraneCell BiologyGolgi apparatusEpitheliumCell biologyDithiothreitolClusterinmedicine.anatomical_structureSecretory proteinchemistrysymbolsOxidation-ReductionProtein Processing Post-TranslationalMolecular ChaperonesJournal of Biological Chemistry
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Phylogenetic profiling and cellular analyses of ARL16 reveal roles in traffic of IFT140 and INPP5E

2021

ABSTRACTThe ARF family of regulatory GTPases is ancient, with 16 members predicted to have been present in the last eukaryotic common ancestor. Our phylogenetic profiling of paralogs in diverse species identified four family members whose presence correlates with that of a cilium/flagellum: ARL3, ARL6, ARL13, and ARL16. No prior evidence links ARL16 to cilia or other cell functions, despite its presence throughout eukaryotes. Deletion of ARL16 in MEFs results in decreased ciliogenesis yet increased ciliary length. We also found Arl16 KO in MEFs to alter ciliary protein content, including loss of ARL13B, ARL3, INPP5E, and the IFT-A core component IFT140. Instead, both INPP5E and IFT140 accum…

Protein contentsymbols.namesakeCiliumCiliogenesisINPP5EsymbolsPhylogenetic profilingGTPaseGolgi apparatusBiologyFlagellumCell biology
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Identification of Trans-Golgi Network Proteins in Arabidopsis thaliana Root Tissue

2014

Knowledge of protein subcellular localization assists in the elucidation of protein function and understanding of different biological mechanisms that occur at discrete subcellular niches. Organelle-centric proteomics enables localization of thousands of proteins simultaneously. Although such techniques have successfully allowed organelle protein catalogues to be achieved, they rely on the purification or significant enrichment of the organelle of interest, which is not achievable for many organelles. Incomplete separation of organelles leads to false discoveries, with erroneous assignments. Proteomics methods that measure the distribution patterns of specific organelle markers along densit…

ProteomicsArabidopsis thalianaArabidopsisorganelle proteomicsProteomicsPlant RootsBiochemistryArticlesymbols.namesakeArtificial IntelligenceTandem Mass SpectrometryArabidopsisOrganelleArabidopsis thalianaChromatography Reverse-PhaseimmunoisolationbiologyArabidopsis Proteinstrans-Golgi networkGeneral ChemistryGolgi apparatusbiology.organism_classificationSubcellular localizationLOPITCell biologyIsobaric labelingphenoDiscomachine learningsymbolsIdentification (biology)Journal of Proteome Research
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