Search results for "Protein transport"

showing 10 items of 197 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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Thioredoxin (Trxo1) interacts with proliferating cell nuclear antigen (PCNA) and its overexpression affects the growth of tobacco cell culture.

2017

Thioredoxins (Trxs), key components of cellular redox regulation, act by controlling the redox status of many target proteins, and have been shown to play an essential role in cell survival and growth. The presence of a Trx system in the nucleus has received little attention in plants, and the nuclear targets of plant Trxs have not been conclusively identified. Thus, very little is known about the function of Trxs in this cellular compartment. Previously, we studied the intracellular localization of PsTrxo1 and confirmed its presence in mitochondria and, interestingly, in the nucleus under standard growth conditions. In investigating the nuclear function of PsTrxo1 we identified proliferati…

0106 biological sciences0301 basic medicineTFs transcription factorsOverexpressionBiologíaBiFC bimolecular fluorescence complementationClinical BiochemistryCell Culture TechniquesTobacco BY-2 cells01 natural sciencesBiochemistryTBY-2 tobacco bright yellow-2DTT 14-dithiothreitolBimolecular fluorescence complementationThioredoxinsGene Expression Regulation PlantTrx thioredoxinlcsh:QH301-705.5GFP green fluorescent proteinlcsh:R5-920biologyProliferating cell nuclear antigen (PCNA)Cell cycleGlutathione3. Good healthCell biologyMitochondriaNTR NADPH thioredoxin reductaseProtein TransportDEM diethyl maleateRT-qPCR Reverse transcription quantitative polymerase chain reactionThioredoxinlcsh:Medicine (General)Oxidation-ReductionAMS 4-acetamido-4-maleimidylstilbene-22-disulfonic acidResearch PaperPCNA proliferating cell nuclear antigenOex overexpressingCell cycleNucleusThioredoxin o103 medical and health sciencesROS reactive oxygen speciesDownregulation and upregulationProliferating Cell Nuclear AntigenTobaccoDAPI 46-diamidine-2-phenylindolmCBM monochlorobimaneCellular compartmentCell NucleusCell growthOrganic ChemistryBotánicaPeasMolecular biologyYFP yellow fluorescent proteinProliferating cell nuclear antigenTBS Tris-buffered salineOD optical density030104 developmental biologylcsh:Biology (General)Cell cultureRNA reactive nitrogen speciesbiology.proteinPrx peroxiredoxinBSA bovine serum albumin010606 plant biology & botanyRedox biology
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AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7

2005

AbstractIn plant chloroplasts two superoxide dismutase (SOD) activities occur, FeSOD and Cu/ZnSOD, with reciprocal regulation in response to copper availability. This system presents a unique model to study the regulation of metal-cofactor delivery to an organelle. The Arabidopsis thaliana gene AtCCS encodes a functional homolog to yeast Ccs1p/Lys7p, a copper chaperone for SOD. The AtCCS protein was localized to chloroplasts where it may supply copper to the stromal Cu/ZnSOD. AtCCS mRNA expression levels are upregulated in response to Cu-feeding and senescence. We propose that AtCCS expression is regulated to allow the most optimal use of Cu for photosynthesis.

0106 biological sciencesCu/Zn superoxide dismutaseChloroplastsSaccharomyces cerevisiae ProteinsMolecular Sequence DataArabidopsisBiophysicsSaccharomyces cerevisiaeMetallo chaperoneChloroplastModels Biological01 natural sciencesBiochemistryGreen fluorescent proteinSuperoxide dismutase03 medical and health sciencesDownregulation and upregulationGene Expression Regulation PlantStructural BiologyOrganelleGeneticsAmino Acid SequenceRNA MessengerMolecular BiologyGene030304 developmental biology0303 health sciencesbiologyArabidopsis ProteinsGene Expression ProfilingGenetic Complementation TestCell BiologyYeastChloroplastProtein TransportBiochemistryChaperone (protein)Mutationbiology.proteinSequence AlignmentCopperMolecular Chaperones010606 plant biology & botanyFEBS Letters
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p24 Family Proteins Are Involved in Transport to the Plasma Membrane of GPI-Anchored Proteins in Plants

2020

p24 proteins are a family of type-I membrane proteins that cycle between the endoplasmic reticulum (ER) and the Golgi apparatus via Coat Protein I (COPI)- and COPII-coated vesicles. These proteins have been proposed to function as cargo receptors, but the identity of putative cargos in plants is still elusive. We previously generated an Arabidopsis (Arabidopsis thaliana) quadruple loss-of-function mutant affecting p24 genes from the δ-1 subclass of the p24 delta subfamily (p24δ3δ4δ5δ6 mutant). This mutant also had reduced protein levels of other p24 family proteins and was found to be sensitive to salt stress. Here, we used this mutant to test the possible involvement of p24 proteins in the…

0106 biological sciencesGenotypePhysiologyGlycosylphosphatidylinositolsMutantArabidopsisGolgi ApparatusPlant ScienceEndoplasmic Reticulum01 natural sciencessymbols.namesakeArabidopsisGeneticsArabidopsis thalianaResearch ArticlesbiologyChemistryArabidopsis ProteinsVesicleEndoplasmic reticulumCell MembraneGenetic VariationMembrane ProteinsCOPIGolgi apparatusbiology.organism_classificationCell biologyProtein TransportMembrane proteinMutationsymbols010606 plant biology & botany
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Protein actors sustaining arbuscular mycorrhizal symbiosis: underground artists break the silence

2013

'Summary' 26 I. 'Casting for a scenario' 26 II. 'Nominees for a preliminary role' 27 III. 'Nominees for a leading role' 32 IV. 'Future artists' 37   'Acknowledgements' 38   References 38 Summary The roots of most land plants can enter a relationship with soil-borne fungi belonging to the phylum Glomeromycota. This symbiosis with arbuscular mycorrhizal (AM) fungi belongs to the so-called biotrophic interactions, involving the intracellular accommodation of a microorganism by a living plant cell without causing the death of the host. Although profiling technologies have generated an increasing depository of plant and fungal proteins eligible for sustaining AM accommodation and functioning, a …

0106 biological sciencesLASER MICRODISSECTIONPhysiologycarbon (C)phosphorus (P)[SDV]Life Sciences [q-bio]Plant Science01 natural sciencesPlant RootsGlomeromycotaMEDICAGO-TRUNCATULA ROOTSRNA interferenceMycorrhizaeLOTUS-JAPONICUSPlastidsMycorrhizaFUNGUS GLOMUS-INTRARADICESPlant ProteinsGENE-EXPRESSIONGenetics0303 health sciencesGene knockdownFungal proteinPHOSPHATE TRANSPORTERarbuscular mycorrhizaCADMIUM STRESS ALLEVIATIONfood and beveragesSTRIGOLACTONE BIOSYNTHESISArbuscular mycorrhizaEPIDERMAL-CELLSProtein Transportmembranes[SDE]Environmental SciencesSignal TransductionINTRACELLULAR ACCOMMODATIONHyphaeBiologybiotrophyPhosphatesFungal Proteins03 medical and health sciencesSymbiosisBotanyGene silencing[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyGlomeromycotaSymbiosis030304 developmental biologyfungi15. Life on landbiology.organism_classificationCarbonsilencing010606 plant biology & botany
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Systematic analysis of specific and nonspecific auxin effects on endocytosis and trafficking.

2021

Abstract The phytohormone auxin and its directional transport through tissues are intensively studied. However, a mechanistic understanding of auxin-mediated feedback on endocytosis and polar distribution of PIN auxin transporters remains limited due to contradictory observations and interpretations. Here, we used state-of-the-art methods to reexamine the auxin effects on PIN endocytic trafficking. We used high auxin concentrations or longer treatments versus lower concentrations and shorter treatments of natural indole-3-acetic acid (IAA) and synthetic naphthalene acetic acid (NAA) auxins to distinguish between specific and nonspecific effects. Longer treatments of both auxins interfere wi…

0106 biological sciencesPhysiologyEndocytic cycleArabidopsisBREFELDIN-APlant Science01 natural sciencesPROTEIN TRAFFICKINGNaphthaleneacetic AcidsPlant Growth RegulatorsGOLGI-APPARATUSheterocyclic compoundsInternalizationResearch Articlesmedia_commonchemistry.chemical_classification0303 health sciencesAcademicSubjects/SCI01270biologyAcademicSubjects/SCI02288AcademicSubjects/SCI02287AcademicSubjects/SCI02286food and beveragesCorrigendaEndocytosisCell biologyProtein TransportMEMBRANE TRAFFICKINGIntracellulartrans-Golgi NetworkGNOM ARF-GEFAcademicSubjects/SCI01280media_common.quotation_subjectEndocytosisClathrin03 medical and health sciencesAuxinGeneticsEndomembrane systemVACUOLAR TRAFFICKINGPLANT030304 developmental biologyIndoleacetic AcidsArabidopsis ProteinsMEDIATES ENDOCYTOSISCell MembraneBiology and Life SciencesTransporterTRANSPORTchemistrybiology.proteinARABIDOPSIS-THALIANA010606 plant biology & botanyPlant physiology
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Distinct lytic vacuolar compartments are embedded inside the protein storage vacuole of dry and germinating Arabidopsis thaliana seeds.

2011

International audience; Plant cell vacuoles are diverse and dynamic structures. In particular, during seed germination, the protein storage vacuoles are rapidly replaced by a central lytic vacuole enabling rapid elongation of embryo cells. In this study, we investigate the dynamic remodeling of vacuolar compartments during Arabidopsis seed germination using immunocytochemistry with antibodies against tonoplast intrinsic protein (TIP) isoforms as well as proteins involved in nutrient mobilization and vacuolar acidification. Our results confirm the existence of a lytic compartment embedded in the protein storage vacuole of dry seeds, decorated by γ-TIP, the vacuolar proton pumping pyrophospha…

0106 biological sciencesPhysiologyProtein storage vacuoleProton-pumping pyrophosphataseArabidopsisPlant ScienceVacuoleUNIQUEMESH: Protein Isoforms01 natural sciencesPYROPHOSPHATASEArabidopsisProtein IsoformsMESH: ArabidopsisH+-ATPASETONOPLAST INTRINSIC PROTEINPLANT-CELLSCation Transport ProteinsIN-VIVOPlant Proteinschemistry.chemical_classification0303 health sciencesMESH: Plant ProteinsGeneral MedicineCell biologyProtein TransportVacuolar acidificationLytic cycleSeedsPREVACUOLAR COMPARTMENTMESH: DesiccationVacuolar Proton-Translocating ATPasesMESH: Protein TransportMESH: Vacuolar Proton-Translocating ATPasesGerminationMESH: Arabidopsis ProteinsMESH: GerminationBiologyAquaporinsMESH: Vacuoles03 medical and health sciencesMESH: AquaporinsMESH: Cation Transport ProteinsStorage protein[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyLytic vacuoleDesiccation030304 developmental biologySeedArabidopsis ProteinsCell Biologybiology.organism_classificationTRANSPORTchemistryMESH: SeedsVacuolesVacuoleMEMBRANEMOBILIZATION010606 plant biology & botany
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The plasma membrane oxidase NtrbohD is responsible for AOS production in elicited tobacco cells

2002

Summary A cDNA encoding a protein, NtrbohD, located on the plasma membrane and homologue to the flavocytochrome of the neutrophil NADPH oxidase, was cloned in tobacco. The corresponding mRNA was accumulated when tobacco leaves and cells were treated with the fungal elicitor cryptogein. After elicitation with cryptogein, tobacco cells transformed with antisense constructs of NtrbohD showed the same extracellular alkalinization as the control, but no longer produced active oxygen species (AOS). This work represents the first demonstration of the function of a homologue of gp91–phox in AOS production in elicited tobacco cells.

0106 biological sciencesTime FactorsNicotiana tabacumMolecular Sequence DataPlant ScienceBiologyGenes Plant01 natural sciencesFungal Proteins[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciences[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsComplementary DNATobaccoGene expressionGeneticsExtracellularAOSAmino Acid SequenceRNA MessengerCells CulturedComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesOxidase testNADPH oxidaseGene Expression ProfilingAlgal ProteinsCell MembraneHydrogen PeroxideCell BiologyHydrogen-Ion ConcentrationPlants Genetically Modifiedbiology.organism_classification3. Good healthElicitorCell biologyPlant LeavesProtein TransportBiochemistryCell culturebiology.proteinOxidoreductasesReactive Oxygen Species010606 plant biology & botany
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AMPA receptor complex constituents: Control of receptor assembly, membrane trafficking and subcellular localization

2018

Fast excitatory transmission at synapses of the central nervous system is mainly mediated by AMPA receptors (AMPARs). Synaptic AMPAR number and function correlates with synaptic strength. AMPARs are thus key proteins of activity-dependent plasticity in neuronal communication. Up- or down-regulation of synaptic AMPAR number is a tightly controlled dynamic process that involves export of receptors from the endoplasmic reticulum (ER) and Golgi apparatus, exocytosis and endocytosis as well as lateral diffusion of the receptors in the cell membrane. The four AMPAR subunits are embedded into a dynamic network of more than 30 interacting proteins. Many of these proteins are known to modulate recep…

0301 basic medicineAMPA receptorBiologyEndocytosisAxonal TransportExocytosis03 medical and health sciencesCellular and Molecular Neurosciencesymbols.namesakeAnimalsHumansReceptors AMPAReceptorMolecular BiologyNeuronsmusculoskeletal neural and ocular physiologyEndoplasmic reticulumCell BiologyGolgi apparatusSubcellular localizationCell biologyTransport proteinProtein Transport030104 developmental biologynervous systemSynapsessymbolsProtein MultimerizationGuanylate KinasesMolecular and Cellular Neuroscience
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Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles.

2018

Abstract Background Virtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization…

0301 basic medicineAlix (also known as PDCD6IP)Protein ConformationLipoylationLipid BilayersBiophysicsSkeletal muscle cellsCell Cycle ProteinsExosomesBiochemistryExosomeTetraspanin 29Cell Line03 medical and health sciencesExtracellular VesiclesPalmitoylationTetraspaninExtracellularHumansLipid bilayerMuscle SkeletalMolecular BiologyCells CulturedEndosomal Sorting Complexes Required for TransportChemistryVesicleCalcium-Binding ProteinsCell MembraneExtracellular vesicleTetraspaninSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cell biologyExosomeProtein Transport030104 developmental biologyS-palmitoylationMembrane proteinextracellular vesicles (EVs)Skeletal muscle cellProtein Processing Post-TranslationalProtein BindingSignal TransductionBiochimica et biophysica acta. General subjects
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