Search results for "Endocytic cycle"

showing 8 items of 58 documents

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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Capture of extracellular zinc ions by astrocytes.

2006

Synaptic zinc ions released during synaptic transmission interact with pre- and postsynaptic neuroreceptors, thus modulating neurotransmission. It is likely that they have to be efficiently cleared from the extracellular milieu to assure subsequent synaptic events. Both neurons and glia are assumed to participate in this clearance by mechanisms that are not fully understood. In this study, electron microscopic zinc cytochemistry has shown zinc-electrondense particles associated with hippocampal astrocytic membranes frequently found accumulated in stacked lamellae. In cultured astrocytes, the use of zinc fluorochromes and endocytic markers allowed the simultaneous imaging of the capture of e…

SucroseEndosomeEndocytic cyclechemistry.chemical_elementZincEndosomesNeurotransmissionBiologyCellular and Molecular NeuroscienceGlial Fibrillary Acidic ProteinmedicineExtracellularAnimalsHomeostasisCells CulturedOrganellesDose-Response Relationship DrugImmunohistochemistryMicroscopy ElectronZincmedicine.anatomical_structureNeurologychemistryAstrocytesBiophysicsCytochemistryNeurogliaRabbitsExtracellular SpaceNeuroscienceAstrocyteGlia
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Echovirus 1 Endocytosis into Caveosomes Requires Lipid Rafts, Dynamin II, and Signaling EventsV⃞

2004

Binding of echovirus 1 (EV1, a nonenveloped RNA virus) to the α2β1 integrin on the cell surface is followed by endocytic internalization of the virus together with the receptor. Here, video-enhanced live microscopy revealed the rapid uptake of fluorescently labeled EV1 into mobile, intracellular structures, positive for green fluorescent protein-tagged caveolin-1. Partial colocalization of EV1 with SV40 (SV40) and cholera toxin, known to traffic via caveosomes, demonstrated that the vesicles were caveosomes. The initiation of EV1 infection was dependent on dynamin II, cholesterol, and protein phosphorylation events. Brefeldin A, a drug that prevents SV40 transport, blocked the EV1 infection…

SucroseTime FactorsvirusesEndocytic cycleDynamin IIchemistry.chemical_compoundDynamin IIPhosphorylationInternalizationCytoskeletonIn Situ HybridizationIn Situ Hybridization Fluorescencemedia_commonGenes Dominant0303 health sciencesMicroscopy Videobiology030302 biochemistry & molecular biologyArticlesBrefeldin AEndocytosisCell biologyEnterovirus B HumanCholesterolRNA ViralElectrophoresis Polyacrylamide GelProtein BindingSignal TransductionCholera Toxinmedia_common.quotation_subjectIntegrinGreen Fluorescent ProteinsImmunoblottingEndocytosisTransfectionCell Line03 medical and health sciencesCapsidMembrane MicrodomainsViral entryCentrifugation Density GradientAnimalsMolecular Biology030304 developmental biologyBinding SitesBrefeldin ACell MembraneCell BiologyKineticschemistryViral replicationMicroscopy Fluorescencebiology.protein
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Membrane transport in the endocytic pathway: Animal versus plant cells

2000

The endocytic pathway is a well established process in animal cells, but it is not well understood in plant cells. At the morphological level, all the compartments involved in endocytosis in animal cells seem to have counterparts in plant cells, and the organization of the pathway appears to share some striking similarities. Several Rab homologues have been found in plant cells, including homologues of Rab5, Rab7, and Rab11, markers of endocytic compartments in animal cells. Coat proteins are also present in plant cells, including clathrin, adaptins, and ADP ribosylation factor proteins. However, endocytic compartments in plant cells also exhibit specific features both in organization and f…

biologyADP ribosylation factorfungiEndocytic cyclefood and beveragesCell BiologyPlant ScienceGeneral MedicineMembrane transportPlant cellEndocytosisClathrinCell biologyBiochemistrybiology.proteinRabFunction (biology)Protoplasma
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The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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α-secretase mediated conversion of the amyloid precursor protein derived membrane stub C99 to C83 limits Aβ generation

2009

The Swedish mutation within the amyloid precursor protein (APP) causes early-onset Alzheimer's disease due to increased cleavage of APP by BACE1. While beta-secretase shedding of Swedish APP (APPswe) largely results from an activity localized in the late secretory pathway, cleavage of wild-type APP occurs mainly in endocytic compartments. However, we show that liberation of Abeta from APPswe is still dependent on functional internalization from the cell surface. Inspite the unchanged overall beta-secretase cleaved soluble APP released from APP(swe) secretion, mutations of the APPswe internalization motif strongly reduced C99 levels and substantially decreased Abeta secretion. We point out t…

medicine.medical_specialtymedia_common.quotation_subjectEndocytic cycleCHO CellsTransfectionBiochemistryAmyloid beta-Protein PrecursorCellular and Molecular NeuroscienceCricetulusCricetinaeInternal medicinemental disordersmedicineAmyloid precursor proteinAnimalsHumansBiotinylationProtein Interaction Domains and MotifsSecretionInternalizationSecretory pathwaymedia_commonAmyloid beta-PeptidesbiologyChemistryP3 peptidePeptide FragmentsCell biologyEndocrinologyGene Expression RegulationAlpha secretaseMutationbiology.proteinAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseJournal of Neurochemistry
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Internalization of novel non-viral vector TAT-streptavidin into human cells

2007

BMC Biotechnology, 7 (1)

virusesEndocytic cyclePROTEINS + POLYPEPTIDES (BIOCHEMISTRY)02 engineering and technologyei-virusperäinen vektoriProtein EngineeringgeeniterapiaPost Transductionchemistry.chemical_compoundTHERAPIES + THERAPEUTICS (MEDICINE)Drug Delivery SystemsLääketieteen bioteknologia - Medical biotechnologyInternalizationmedia_commoninfo:eu-repo/classification/ddc/5700303 health sciencesPinocytosisNocodazoleVEKTOREN (GENETISCHE TECHNIKEN)021001 nanoscience & nanotechnologyLife sciencesCell biologyEndosomal EscapeBiotinylationGene Products tatVirusesVECTORS (GENETIC TECHNIQUES)VEKTOREN (GENETISCHE TECHNIKEN); THERAPIEN + THERAPEUTIK (MEDIZIN); PROTEINE + POLYPEPTIDE (BIOCHEMIE); VECTORS (GENETIC TECHNIQUES); THERAPIES + THERAPEUTICS (MEDICINE); PROTEINS + POLYPEPTIDES (BIOCHEMISTRY)0210 nano-technologyTHERAPIEN + THERAPEUTIK (MEDIZIN)BiotechnologyResearch ArticleStreptavidinEndosomeImmunoelectron microscopymedia_common.quotation_subjectRecombinant Fusion Proteinslcsh:BiotechnologyGenetic VectorsBiologyEndocytosis03 medical and health sciencesstreptavidiiniddc:570lcsh:TP248.13-248.65HumansEndosomal Marker030304 developmental biologyMolecular biologyEndocytic VesiclechemistryStreptavidinTATPROTEINE + POLYPEPTIDE (BIOCHEMIE)HeLa CellsBMC Biotechnology
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Human Papillomavirus Types 16, 18, and 31 Share Similar Endocytic Requirements for Entry

2013

ABSTRACT Human papillomavirus type 18 (HPV18), one of the HPVs with malignant potential, enters cells by an unknown endocytic mechanism. The key cellular requirements for HPV18 endocytosis were tested in comparison to those for HPV16 and -31 endocytoses. HPV18 (like HPV16 and -31) entry was independent of clathrin, caveolin, dynamin, and lipid rafts but required actin polymerization and tetraspanin CD151, and the viruses were routed to the same LAMP-1-positive compartment. Hence, the viruses shared similar cellular requirements for endocytic entry.

virusesImmunologyEndocytic cycleTetraspanin 24EndocytosisMicrobiologyClathrinDynamin IIPolymerizationDynamin IIMembrane MicrodomainsTetraspaninVirologyCaveolinHumansHuman papillomavirus 31Lipid raftDynaminHuman papillomavirus 16Microscopy ConfocalHuman papillomavirus 18biologyvirus diseasesLysosome-Associated Membrane GlycoproteinsVirus InternalizationVirologyActinsEndocytosisVirus-Cell InteractionsCell biologyMicroscopy ElectronMicroscopy FluorescenceInsect Sciencebiology.proteinElectrophoresis Polyacrylamide GelHeLa CellsJournal of Virology
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