Search results for "ENDOCYTOSIS"

showing 10 items of 185 documents

Reconstitution of vesicular transport to Rab11-positive recycling endosomes in vitro.

2003

Rab GTPases are key regulators of vesicular protein transport in both the endocytic and exocytic pathways. In endocytosis and recycling, Rab11 plays a role in receptor recycling to plasma membrane via the pericentriolar recycling compartment. However, little is known about the molecular requirements and partners that promote transport through Rab11-positive recycling endosomes. Here, we report a novel approach to reconstitute transport to immunoabsorbed recycling endosomes in vitro. We show that transport is temperature-, energy-, and time-dependent and requires the presence of Rab proteins, as it is inhibited by the Rab-interacting protein Rab GDP-dissociation inhibitor that removes Rab pr…

Receptor recyclingCytochalasin DEndosomeEndocytic cycleBiophysicsVesicular Transport ProteinsCHO CellsEndosomesEndocytosisBiochemistryCricetulusCricetinaeReceptors TransferrinAnimalsVesicular Protein TransportTransport VesiclesMolecular BiologyGuanine Nucleotide Dissociation InhibitorsChemistryCell BiologyActin cytoskeletonAdaptation PhysiologicalCell biologyVesicular transport proteinProtein Transportrab GTP-Binding ProteinsRabBiochemical and biophysical research communications
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Axon-glia interaction and membrane traffic in myelin formation

2014

In vertebrate nervous systems myelination of neuronal axons has evolved to increase conduction velocity of electrical impulses with minimal space and energy requirements. Myelin is formed by specialized glial cells which ensheath axons with a lipid-rich insulating membrane. Myelination is a multi-step process initiated by axon-glia recognition triggering glial polarization followed by targeted myelin membrane expansion and compaction. Thereby, a myelin sheath of complex subdomain structure is established. Continuous communication between neurons and glial cells is essential for myelin maintenance and axonal integrity. A diverse group of diseases, from multiple sclerosis to schizophrenia, ha…

SNAREsmyelinationcell communicationReview Articlemembrane trafficlcsh:RC321-571570 Life sciencesmyelin diseaseFyn kinasenervous systemendocytosislocal protein synthesislcsh:Neurosciences. Biological psychiatry. NeuropsychiatryNeuroscience570 Biowissenschaften
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Lateral reorganization of plasma membrane is involved in the yeast resistance to severe dehydration

2010

International audience; In this study, we investigated the kinetic and the magnitude of dehydrations on yeast plasma membrane (PM) modifications because this parameter is crucial to cell survival. Functional (permeability) and structural (morphology, ultrastructure, and distribution of the protein Sur7-GFP contained in sterol-rich membrane microdomains) PM modifications were investigated by confocal and electron microscopy after progressive (non-lethal) and rapid (lethal) hyperosmotic perturbations. Rapid cell dehydration induced the formation of many PM invaginations followed by membrane internalization of low sterol content PM regions with time. Permeabilization of the plasma membrane occ…

Saccharomyces cerevisiae Proteins[SDV.BIO]Life Sciences [q-bio]/BiotechnologyRecombinant Fusion Proteinsmedia_common.quotation_subjectCellBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryCell survivallaw.invention[SPI]Engineering Sciences [physics][ SDV.MP ] Life Sciences [q-bio]/Microbiology and ParasitologylawElectron microscopymedicine[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringMicrodomainDehydration kineticInternalizationEisosomemedia_commonDehydrationOsmotic concentrationCell MembraneOsmolar ConcentrationLipid microdomainMembrane ProteinsWaterCell BiologyEndocytosisCell biologyConfocal microscopy[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitologymedicine.anatomical_structureMembraneUltrastructureElectron microscopeBiochimica et Biophysica Acta (BBA) - Biomembranes
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Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-mediated endocytosis.

2014

Item does not contain fulltext The human Usher syndrome (USH) is a complex ciliopathy with at least 12 chromosomal loci assigned to three clinical subtypes, USH1-3. The heterogeneous USH proteins are organized into protein networks. Here, we identified Magi2 (membrane-associated guanylate kinase inverted-2) as a new component of the USH protein interactome, binding to the multifunctional scaffold protein SANS (USH1G). We showed that the SANS-Magi2 complex assembly is regulated by the phosphorylation of an internal PDZ-binding motif in the sterile alpha motif domain of SANS by the protein kinase CK2. We affirmed Magi2's role in receptor-mediated, clathrin-dependent endocytosis and showed tha…

Scaffold proteinGuanylate kinaseMolecular Sequence DataPrimary Cell CultureNerve Tissue ProteinsBiologyEndocytosisPhotoreceptor cellExocytosisMiceCiliogenesisGeneticsmedicineAnimalsHumansProtein Interaction Domains and MotifsAmino Acid SequencePhosphorylationRNA Small InterferingSensory disorders Radboud Institute for Molecular Life Sciences [Radboudumc 12]Molecular BiologyGenetics (clinical)Adaptor Proteins Signal TransducingBinding SitesGeneral MedicineClathrinEndocytosisCell biologyMice Inbred C57BLRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]medicine.anatomical_structureHEK293 CellsGene Expression RegulationCiliary pocketCarrier ProteinsSterile alpha motifGuanylate KinasesSequence AlignmentUsher SyndromesPhotoreceptor Cells VertebrateProtein BindingSignal TransductionHuman molecular genetics
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Direct binding of Magi2 to the USH1G protein SANS links the periciliary USH protein network to endocytosis

2012

The human Usher syndrome (USH) is the most common form of combined deaf-blindness. The encoded molecules are integrated into protein networks by scaffolds including the USH1G protein SANS (scaffold protein containing ankyrin repeats and SAM domain). Previous studies indicated SANS´ participation in vesicle transport and cargo handover at the periciliary region of photoreceptor cells. To decipher the precise cellular role of SANS, we searched for interacting partners. Therefore we adopted a yeast-2-hybrid screen of a retinal cDNA library using SANS´ C-terminus as bait. Amongst others we identified the MAGUK protein Magi2 (membrane-associated guanylate kinase inverted-2) as putative binding p…

Scaffold proteinImmunoelectron microscopyCell BiologyBiologyEndocytosisInteractomePhotoreceptor cellCell biologyVesicular transport proteinmedicine.anatomical_structureCiliary pocketPoster PresentationmedicineAnkyrin repeatCilia
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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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Tuning the surface of nanoparticles: Impact of poly(2-ethyl-2-oxazoline) on protein adsorption in serum and cellular uptake

2016

Item does not contain fulltext Due to the adsorption of biomolecules, the control of the biodistribution of nanoparticles is still one of the major challenges of nanomedicine. Poly(2-ethyl-2-oxazoline) (PEtOx) for surface modification of nanoparticles is applied and both protein adsorption and cellular uptake of PEtOxylated nanoparticles versus nanoparticles coated with poly(ethylene glycol) (PEG) and non-coated positively and negatively charged nanoparticles are compared. Therefore, fluorescent poly(organosiloxane) nanoparticles of 15 nm radius are synthesized, which are used as a scaffold for surface modification in a grafting onto approach. With multi-angle dynamic light scattering, asym…

SerumTime FactorsPolymers and PlasticsSurface PropertiesNanoparticleBioengineeringProtein Corona02 engineering and technologyChemical Fractionation010402 general chemistry01 natural sciencesCell LineBiomaterialschemistry.chemical_compoundAdsorptionDynamic light scatteringMaterials ChemistryPolyaminesOrganic chemistryHumanspoly(2-ethyl-2-oxazoline)Particle SizeElectrophoresis Agar Gelpoly(ethylene glycol)RhodaminesProteinscellular uptake021001 nanoscience & nanotechnologyprotein adsorptionDynamic Light ScatteringEndocytosis0104 chemical scienceschemistryChemical engineeringSurface modificationNanomedicineInstitut für ChemienanoparticlesAdsorption0210 nano-technologyEthylene glycolNanomedicine Radboud Institute for Molecular Life Sciences [Radboudumc 19]BiotechnologyProtein adsorption
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Tetraspanin CD151 Mediates Papillomavirus Type 16 Endocytosis

2013

ABSTRACT Human papillomavirus type 16 (HPV16) is the primary etiologic agent for cervical cancer. The infectious entry of HPV16 into cells occurs via a so-far poorly characterized clathrin- and caveolin-independent endocytic pathway, which involves tetraspanin proteins and actin. In this study, we investigated the specific role of the tetraspanin CD151 in the early steps of HPV16 infection. We show that surface-bound HPV16 moves together with CD151 within the plane of the membrane before they cointernalize into endosomes. Depletion of endogenous CD151 did not affect binding of viral particles to cells but resulted in reduction of HPV16 endocytosis. HPV16 uptake is dependent on the C-termina…

Small interfering RNAEndosomevirusesmedia_common.quotation_subjectDNA Mutational AnalysisImmunologyEndocytic cycleIntegrinTetraspanin 24EndocytosisMicrobiologyClathrinCell LineTetraspaninVirologyHumansInternalizationmedia_commonHuman papillomavirus 16integumentary systembiologyvirus diseasesVirus InternalizationMolecular biologyEndocytosisfemale genital diseases and pregnancy complicationsVirus-Cell InteractionsCell biologyGene Knockdown TechniquesInsect Sciencebiology.proteinMutant ProteinsJournal of Virology
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Internalization of coxsackievirus A9 is mediated by {beta}2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin.

2010

ABSTRACT Coxsackievirus A9 (CAV9) is a member of the human enterovirus B species within the Enterovirus genus of the family Picornaviridae . It has been shown to utilize αV integrins, particularly αVβ6, as its receptors. The endocytic pathway by which CAV9 enters human cells after the initial attachment to the cell surface has so far been unknown. Here, we present a systematic study concerning the internalization mechanism of CAV9 to A549 human lung carcinoma cells. The small interfering RNA (siRNA) silencing of integrin β6 subunit inhibited virus proliferation, confirming that αVβ6 mediates the CAV9 infection. However, siRNAs against integrin-linked signaling molecules, such as Src, Fyn, R…

Small interfering RNAmedia_common.quotation_subjectImmunologyEndocytic cycleIntegrinCaveolin 1CoxsackievirusEndocytosisCaveolaeMicrobiologyClathrinAmilorideDynamin IIVirologyCell Line TumorHumansRNA Small InterferingInternalizationmedia_commonDynaminbiologyADP-Ribosylation FactorsVirus Internalizationbiology.organism_classificationMolecular biologyClathrinEndocytosisCell biologyEnterovirus B HumanVirus-Cell InteractionsADP-Ribosylation Factor 6Insect Sciencebiology.proteinPinocytosisbeta 2-MicroglobulinJournal of virology
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Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis

2008

Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes.

Staphylococcus aureusEndosomeBacterial ToxinsBiophysicsEndosomesBiologyEndocytosisHemolysin ProteinsBiochemistryα-ToxinExocytosisVirulence factorExocytosisCell LineHemolysin ProteinsStructural BiologyNucleated cellChlorocebus aethiopsGeneticsExtracellularAnimalsHumansMolecular BiologyCell NucleusBacterial pore forming toxinPore-forming toxinInnate defence mechanismCell BiologyEndocytosisCell biologyExosomeBiochemistryCOS CellsMutationMacrolidesFEBS Letters
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