Search results for "Vesicular Transport"

showing 5 items of 55 documents

PHD3 regulates EGFR internalization and signalling in tumours

2014

Tumours exploit their hypoxic microenvironment to induce a more aggressive phenotype, while curtailing the growth-inhibitory effects of hypoxia through mechanisms that are poorly understood. The prolyl hydroxylase PHD3 is regulated by hypoxia and plays an important role in tumour progression. Here we identify PHD3 as a central regulator of epidermal growth factor receptor (EGFR) activity through the control of EGFR internalization to restrain tumour growth. PHD3 controls EGFR activity by acting as a scaffolding protein that associates with the endocytic adaptor Eps15 and promotes the internalization of EGFR. In consequence, loss of PHD3 in tumour cells suppresses EGFR internalization and hy…

Scaffold proteinmedia_common.quotation_subjectEndocytic cycleRegulatorGeneral Physics and AstronomyGeneral Biochemistry Genetics and Molecular BiologyHypoxia-Inducible Factor-Proline DioxygenasesCell Line TumorNeoplasmsmedicineHumansEpidermal growth factor receptorInternalizationmedia_commonCell ProliferationMultidisciplinarybiologyCell growthChemistryGeneral ChemistryHypoxia (medical)EndocytosisCell biologyErbB ReceptorsGene Expression Regulation NeoplasticAdaptor Proteins Vesicular TransportSignallingbiology.proteinmedicine.symptomProtein BindingSignal Transduction
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The Synapse-Like Interaction between Chloroplast, dictyosome, and Other Cell Compartments during Increased Ethylene Production in Leaves of Rye (Seca…

2000

Rye (Secale cereale L.) plants were treated with an ethylene releaser ethephon (2-chloroethylphosphonic acid) in concentration of 4×10−2 M. We studied electron microscopically, if and how chloroplasts interact with well-documented sites of ethylene production/binding, i.e., with endoplasmic reticulum, dictyosomes, mitochondria, plasma membrane, and tonoplast. During the sharp increase of ethylene synthesis in mesophyll cells of rye leaves, the direct local continguity of chloroplast envelope or envelope protrusions with the above mentioned cell compartments was typical. Moreover, a large number and diversity of versatile chloroplast-dictyosome associations were conspicuous, in which both th…

SecalePhysiologyEndoplasmic reticulumfood and beveragesPlant ScienceVacuoleGolgi apparatusBiologybiology.organism_classificationChloroplast membraneApoplastChloroplastVesicular transport proteinsymbols.namesakeBiochemistryBiophysicssymbolsPhotosynthetica
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Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs

2013

AbstractExit from the Endoplasmic Reticulum (ER) of newly synthesized proteins is mediated by COPII vesicles that bud from the ER at the ER Exit Sites (ERESs). Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Previously, we demonstrated that ER stress rapidly impairs the formation of COPII vesicles. Here, we show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER.

Vesicular Transport ProteinsBiophysicsEndoplasmic ReticulumBiochemistryCell LineVesicular Transport ProteinGeneticStructural BiologyERESGeneticsVesicular Transport ProteinsHumansCOPIIEndoplasmic Reticulum StreMolecular BiologyCOPIIChemistryVesicleEndoplasmic reticulumSec23Cell BiologyCOP-Coated VesiclesSEC23AEndoplasmic Reticulum StressCell biologyBiophysicUnfolded protein responseER streProtein foldingCOP-Coated VesiclesER stressCOP-Coated VesicleHumanProtein BindingFEBS Letters
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Immunoelectron Microscopy of Vesicle Transport to the Primary Cilium of Photoreceptor Cells

2009

Cilia are organelles of high structural complexity. Since the biosynthetic machinery is absent from cilia all their molecular components must be synthesized in organelles of the cytoplasm and subsequently transported to the cilium. Ciliary cargos are thought to be translocated in the membrane of transport vesicles or association with these vesicles to the base of the cilium where the vesicles fuse with the periciliary target membrane for further delivery of their cargo into the ciliary compartment by the intraflagellar transport (IFT). Here we describe a modified preembedding labeling method as an alternative technique to conventional postembedding methods eligible for analyses of ciliary c…

Vesicular transport proteinImmunolabelingCytoplasmIntraflagellar transportCiliumVesicleImmunoelectron microscopyOrganellesense organsBiologyCell biology
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Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules.

2004

AbstractPolyglutamine expansion (polyQ) in the protein huntingtin is pathogenic and responsible for the neuronal toxicity associated with Huntington's disease (HD). Although wild-type huntingtin possesses antiapoptotic properties, the relationship between the neuroprotective functions of huntingtin and pathogenesis of HD remains unclear. Here, we show that huntingtin specifically enhances vesicular transport of brain-derived neurotrophic factor (BDNF) along microtubules. Huntingtin-mediated transport involves huntingtin-associated protein-1 (HAP1) and the p150Glued subunit of dynactin, an essential component of molecular motors. BDNF transport is attenuated both in the disease context and b…

congenital hereditary and neonatal diseases and abnormalitiesHuntingtinCell SurvivalContext (language use)Nerve Tissue ProteinsMicrotubulesModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyMiceNeurotrophic factorsmental disordersHuntingtin ProteinAnimalsCells CulturedNeuronsHuntingtin ProteinbiologyBiochemistry Genetics and Molecular Biology(all)Huntingtin-associated protein 1Brain-Derived Neurotrophic FactorCytoplasmic VesiclesBrainNuclear ProteinsBiological TransportDynactin ComplexCell biologynervous system diseasesVesicular transport proteinDNA-Binding ProteinsBiochemistrynervous systembiology.proteinDynactinMicrotubule-Associated ProteinsNeurotrophinCell
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