Search results for "secretory pathway."

showing 10 items of 41 documents

Loss of Arabidopsis p24 function affects ERD2 traffic and Golgi structure and activates the unfolded protein response

2017

The p24 family of proteins (also known as the TMED family) are key regulators of protein trafficking along the secretory pathway, but very little is known about their functions in plants. A quadruple loss-of-function mutant affecting the p24 genes from the δ-1 subclass of the p24δ subfamily (p24δ3δ4δ5δ6) showed alterations in the Golgi, suggesting that these p24 proteins play a role in the organization of the compartments of the early secretory pathway in Arabidopsis Loss of p24δ-1 proteins also induced the accumulation of the K/HDEL receptor ERD2a (ER lumen protein-retaining receptor A) at the Golgi and increased secretion of BiP family proteins, ER chaperones containing an HDEL signal, pr…

0106 biological sciences0301 basic medicineEndoplasmic reticulumMutantCell BiologyBiologyGolgi apparatusbiology.organism_classification01 natural sciencesCell biology03 medical and health sciencessymbols.namesake030104 developmental biologyBiochemistryArabidopsissymbolsUnfolded protein responseSecretionCOPIISecretory pathway010606 plant biology & botanyJournal of Cell Science
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Expression of the Intracellular COPT3-Mediated Cu Transport Is Temporally Regulated by the TCP16 Transcription Factor

2018

[EN] Copper is an essential element in plants. When scarce, copper is acquired from extracellular environment or remobilized from intracellular sites, through members of the high affinity copper transporters family COPT located at the plasma membrane and internal membrane, respectively. Here, we show that COPT3 is an intracellular copper transporter, located at a compartment of the secretory pathway, that is mainly expressed in pollen grains and vascular bundles. Contrary to the COPT1 plasma membrane member, the expression of the internal COPT3 membrane transporter was higher at 12 h than at 0 h of a neutral photoperiod day under copper deficiency. The screening of a library of conditionall…

0106 biological sciences0301 basic medicineMutantchemistry.chemical_elementPlant Sciencelcsh:Plant culture01 natural sciencesTCP1603 medical and health sciencesTranscriptional regulationGene expressionBIOQUIMICA Y BIOLOGIA MOLECULARExtracellularmedicinelcsh:SB1-1110COPT3transcriptional regulationheavy metalsTranscription factorSecretory pathwayOriginal ResearchCopper transportmedicine.diseaseCopperCell biology030104 developmental biologyHeavy metalschemistrycopper transportCopper deficiencyIntracellular010606 plant biology & botanyFrontiers in Plant Science
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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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Loss of

2020

The early secretory pathway involves bidirectional transport between the endoplasmic reticulum (ER) and the Golgi apparatus and is mediated by coat protein complex I (COPI)-coated and coat protein complex II (COPII)-coated vesicles. COPII vesicles are involved in ER to Golgi transport meanwhile COPI vesicles mediate intra-Golgi transport and retrograde transport from the Golgi apparatus to the ER. The key component of COPI vesicles is the coatomer complex, that is composed of seven subunits (α/β/β'/γ/δ/ε/ζ). In Arabidopsis two genes coding for the β-COP subunit have been identified, which are the result of recent tandem duplication. Here we have used a loss-of-function approach to study the…

0106 biological sciences0301 basic medicineProtein subunitArabidopsisPlant Sciencelcsh:Plant culture01 natural sciences03 medical and health sciencessymbols.namesakelcsh:SB1-1110coat protein II (COPII)Plantes Cèl·lules i teixitsCOPIICreixement (Plantes)Secretory pathwayOriginal Researchsalt stressChemistryEndoplasmic reticulumVesiclecoat protein I (COPI)plant growthCOPIGolgi apparatusCell biology030104 developmental biologyCoatomerβ-COPGolgi apparatussymbols010606 plant biology & botanyFrontiers in plant science
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Plasma membrane protein trafficking in plant-microbe interactions: a plant cell point of view

2014

International audience; In order to ensure their physiological and cellular functions, plasma membrane (PM) proteins must be properly conveyed from their site of synthesis, i.e., the endoplasmic reticulum, to their final destination, the PM, through the secretory pathway. PM protein homeostasis also relies on recycling and/or degradation, two processes that are initiated by endocytosis. Vesicular membrane trafficking events to and from the PM have been shown to be altered when plant cells are exposed to mutualistic or pathogenic microbes. In this review, we will describe the fine-tune regulation of such alterations, and their consequence in PM protein activity. We will consider the formatio…

0106 biological sciencesplant–microbe interactions[SDV]Life Sciences [q-bio]signaling proteinsplasma membrane;vesicular trafficking;plant-microbe interactions;signaling proteins;sugar transportersReview Articlerécepteur cytoplasmique et nucléairePlant ScienceBiologymembrane plasmiqueSugar transporterslcsh:Plant cultureEndocytosisBioinformaticsplasma membrane01 natural sciencesPlant-Microbe Interactionsvoie secretoire03 medical and health sciences[SDV.BV]Life Sciences [q-bio]/Vegetal Biologylcsh:SB1-1110ReceptorSecretory pathway030304 developmental biologychemistry.chemical_classification0303 health sciencesReactive oxygen speciesphysiologie cellulaire végétaletransport de protéineEndoplasmic reticulumPlant cellTransport proteinCell biologyinteraction protéine membranechemistry[SDE]Environmental Sciencesvesicular traffickingIntracellular010606 plant biology & botanyFrontiers in Plant Science
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LRP1 Modulates APP Intraneuronal Transport and Processing in Its Monomeric and Dimeric State.

2017

The low-density lipoprotein receptor-related protein 1, LRP1, interacts with APP and affects its processing. This is assumed to be mostly caused by the impact of LRP1 on APP endocytosis. More recently, also an interaction of APP and LRP1 early in the secretory pathway was reported whereat retention of LRP1 in the ER leads to decreased APP cell surface levels and in turn, to reduced Aβ secretion. Here, we extended the biochemical and immunocytochemical analyses by showing via live cell imaging analyses in primary neurons that LRP1 and APP are transported only partly in common (one third) but to a higher degree in distinct fast axonal transport vesicles. Interestingly, co-expression of LRP1 a…

0301 basic medicineADAM10amyloid precursor protein (APP)Endocytosislcsh:RC321-57103 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinemental disordersSecretionReceptorMolecular Biologylcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySecretory pathwayOriginal ResearchdimerizationChemistryVesicleLRP1030104 developmental biologyBiochemistrytransportBiophysicsAxoplasmic transportprocessinglow density lipoprotein receptor-related protein 1 (LRP1)030217 neurology & neurosurgeryNeuroscienceFrontiers in molecular neuroscience
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Uptake of polyphosphate microparticles in vitro (SaOS-2 and HUVEC cells) followed by an increase of the intracellular ATP pool size

2017

Recently two approaches were reported that addressed a vitally important problem in regenerative medicine, i. e. the successful treatment of wounds even under diabetic conditions. Accordingly, these studies with diabetic rabbits [Sarojini et al. PLoS One 2017, 12(4):e0174899] and diabetic mice [Müller et al. Polymers 2017, 9, 300] identified a novel (potential) target for the acceleration of wound healing in diabetes. Both studies propose a raise of the intracellular metabolic energy status via exogenous administration either of ATP, encapsulated into lipid vesicles, or of polyphosphate (polyP) micro-/nanoparticles. Recently this physiological polymer, polyP, was found to release metabolic …

0301 basic medicineConfocal MicroscopyBioenergeticsPhysiologyPolymerslcsh:Medicine02 engineering and technologyTrifluoperazineBiochemistryAdenosine TriphosphateEndocrinologyPolyphosphatesSpectroscopy Fourier Transform InfraredMedicine and Health Scienceslcsh:ScienceStainingMicroscopySecretory PathwayMultidisciplinaryChemistryLight MicroscopyCell Staining021001 nanoscience & nanotechnologyEndocytosisMicrospheres3. Good healthCell biologyChemistryMacromoleculesCell ProcessesPhysical SciencesRabbits0210 nano-technologyIntracellularResearch Articlemedicine.drugEndocrine DisordersMaterials by StructureMaterials ScienceBioenergeticsResearch and Analysis MethodsEndocytosisCell Line03 medical and health sciencesTissue RepairDiabetes Mellitusotorhinolaryngologic diseasesmedicineAnimalsHumansCalcium metabolismWound Healinglcsh:RSpectrometry X-Ray EmissionBiology and Life SciencesCell BiologyPolymer Chemistrydigestive system diseasesIn vitroMetabolism030104 developmental biologySpecimen Preparation and TreatmentCell cultureMetabolic DisordersMicroscopy Electron ScanningCalciumlcsh:QEnergy MetabolismPhysiological ProcessesWound healingConfocal Laser MicroscopyPowder DiffractionPLOS ONE
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Phenolic extract from oleaster (Olea europaea var. Sylvestris) leaves reduces colon cancer growth and induces caspase-dependent apoptosis in colon ca…

2017

Erratum inCorrection: Phenolic extract from oleaster (Olea europaea var. Sylvestris) leaves reduces colon cancer growth and induces caspase-dependent apoptosis in colon cancer cells via the mitochondrial apoptotic pathway. [PLoS One. 2017]; International audience; Dietary polyphenols, derived from natural products, have received a great interest for their chemopreventive properties against cancer. In this study, we investigated the effects of phenolic extract of the oleaster leaves (PEOL) on tumor growth in mouse model and on cell death in colon cancer cell lines. We assessed the effect of oleaster leaf infusion on HCT116 (human colon cancer cell line) xenograft growth in athymic nude mice.…

0301 basic medicineLeavesCarcinoma Cellslcsh:MedicineApoptosisPlant ScienceMitochondrionEndoplasmic ReticulumBiochemistry[ SDV.CAN ] Life Sciences [q-bio]/Cancer0302 clinical medicineMedicine and Health SciencesMitochondrial calcium uptakeDiseaselcsh:ScienceEnergy-Producing OrganellesStainingchemistry.chemical_classificationSecretory PathwayMultidisciplinaryCell DeathPlant AnatomyCytochrome cCell StainingAnimal ModelsMitochondriaOlive Leaf ExtractChemistryOncologyExperimental Organism SystemsBiochemistryCell Processes030220 oncology & carcinogenesisPhysical SciencesCellular Structures and OrganellesResearch ArticleProgrammed cell deathActivationMouse Models[SDV.CAN]Life Sciences [q-bio]/CancerBioenergeticsBiologyResearch and Analysis MethodsColorectal-CancerCaspase-Dependent Apoptosis03 medical and health sciencesModel OrganismsPhenolsCytochrome-CColorectal CancerReactive oxygen speciesP53Cell growthProteinlcsh:RChemical CompoundsBiology and Life SciencesCancers and NeoplasmsPolyphenolsCell BiologyMolecular biology030104 developmental biologychemistrySpecimen Preparation and TreatmentApoptosisbiology.proteinCalciumlcsh:QPLoS ONE
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The Effect of a Novel c.820C>T (Arg274Trp) Mutation in the Mitofusin 2 Gene on Fibroblast Metabolism and Clinical Manifestation in a Patient

2017

Charcot-Marie-Tooth disease type 2A (CMT2A) is an autosomal dominant axonal peripheral neuropathy caused by mutations in the mitofusin 2 gene (MFN2). Mitofusin 2 is a GTPase protein present in the outer mitochondrial membrane and responsible for regulation of mitochondrial network architecture via the fusion of mitochondria. As that fusion process is known to be strongly dependent on the GTPase activity of mitofusin 2, it is postulated that the MFN2 mutation within the GTPase domain may lead to impaired GTPase activity, and in turn to mitochondrial dysfunction. The work described here has therefore sought to verify the effects of MFN2 mutation within its GTPase domain on mitochondrial and e…

0301 basic medicineMaleHydrolasesMutantMFN2lcsh:MedicineGTPaseMitochondrionmedicine.disease_causeEndoplasmic ReticulumBiochemistryGTP Phosphohydrolases0302 clinical medicineMental RetardationAnimal CellsCharcot-Marie-Tooth DiseaseMedicine and Health SciencesMissense mutationlcsh:ScienceEnergy-Producing OrganellesCells CulturedConnective Tissue CellsGeneticsMutationMultidisciplinarySecretory PathwayOrganic CompoundsMonosaccharidesTryptophanMitochondrial DNACell biologyMitochondriaEnzymesNucleic acidsChemistryNeurologyConnective TissueCell ProcessesPhysical SciencesCellular Structures and OrganellesCellular TypesAnatomyResearch ArticleForms of DNACarbohydratesMutation MissenseBiologyBioenergeticsArgininePolymorphism Single NucleotideMitochondrial Proteins03 medical and health sciencesMitofusin-2Young AdultmedicineGeneticsHumansEndoplasmic reticulumlcsh:ROrganic ChemistryChemical CompoundsBiology and Life SciencesProteinsCell BiologyDNAFibroblastsGuanosine Triphosphatase030104 developmental biologyBiological TissueGlucoseAmino Acid SubstitutionCase-Control StudiesMutationEnzymologylcsh:Q030217 neurology & neurosurgeryPLoS ONE
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Oligodendrocytes Provide Antioxidant Defense Function for Neurons by Secreting Ferritin Heavy Chain.

2020

An evolutionarily conserved function of glia is to provide metabolic and structural support for neurons. To identify molecules generated by glia and with vital functions for neurons, we used Drosophila melanogaster as a screening tool, and subsequently translated the findings to mice. We found that a cargo receptor operating in the secretory pathway of glia was essential to maintain axonal integrity by regulating iron buffering. Ferritin heavy chain was identified as the critical secretory cargo, required for the protection against iron-mediated ferroptotic axonal damage. In mice, ferritin heavy chain is highly expressed by oligodendrocytes and secreted by employing an unconventional secret…

0301 basic medicineMalePhysiologyAntioxidantsArticlemetabolism [Oligodendroglia]03 medical and health sciencesMyelinMice0302 clinical medicineddc:570medicineAnimalsSecretionReceptorCytotoxicityMolecular BiologySecretory pathwayNeuronsbiologyChemistrymetabolism [Apoferritins]Cell Biologybiology.organism_classificationCell biologyFerritinMice Inbred C57BLOligodendroglia030104 developmental biologymedicine.anatomical_structurenervous systemmetabolism [Neurons]Apoferritinsbiology.proteinmetabolism [Antioxidants]Drosophila melanogaster030217 neurology & neurosurgeryFunction (biology)Cell metabolism
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