Search results for "Clathrin"

showing 10 items of 48 documents

Entry of Human Parechovirus 1

2001

ABSTRACT Human parechovirus 1 (HPEV-1) is a prototype member of parechoviruses, a recently established picornavirus genus. Although there is preliminary evidence that HPEV-1 recognizes α V integrins as cellular receptors, our understanding of early events during HPEV-1 infection is still very limited. The aim of this study was to clarify the entry mechanisms of HPEV-1, including the attachment of the virus onto the host cell surface and subsequent internalization. In blocking experiments with monoclonal antibodies against different receptor candidates, antibodies against α V and β 3 integrin subunits, in particular in combination, appeared to be the most efficient ones in preventing the HPE…

PicornavirusEndosomeImmunologyEndocytic cycleGolgi ApparatusHuman parechovirus 1EndosomesPicornaviridaePlatelet Membrane GlycoproteinsEndoplasmic ReticulumVirus ReplicationCaveolinsMicrobiologyClathrinEEA103 medical and health sciencessymbols.namesakeCapsidAntigens CDVirologyTumor Cells CulturedHumans030304 developmental biologyHost cell surface0303 health sciencesbiology030302 biochemistry & molecular biologyIntegrin beta3Clathrin-Coated VesiclesIntegrin alphaVGolgi apparatusbiology.organism_classificationVirologyClathrinEndocytosisVirus-Cell Interactions3. Good healthCell biologyInsect Sciencesymbolsbiology.proteinReceptors VirusJournal of Virology
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Purification and partial characterization of a lectin protein complex, the clathrilectin, from the calcareous sponge Clathrina clathrus

2016

Carbohydrate-binding proteins were purified from the marine calcareous sponge Clathrina clathrus via affinity chromatography on lactose and N-acetyl glucosamine- agarose resins. Proteomic analysis of acrylamide gel separated protein subunits obtained in reducing conditions pointed out several candidates for lectins. Based on amino- acid sequence similarity, two peptides displayed homology with the jack bean lectin Concanavalin A, 
 including a conserved domain shared by proteins in the L-type lectin superfamily. An N-acetyl glucosamine - binding protein complex, named clathrilectin, was further purified via gel filtration chromatography, bioguided with a diagnostic rabbit erythrocyte haemag…

Proteomics0301 basic medicinePhysiologySyconBiochemistry03 medical and health sciencesAffinity chromatographyLectinsAnimalsTrypsinMolecular Biology030102 biochemistry & molecular biologybiologyCalcareous spongeHemagglutinationLectinClathrina clathrusbiology.organism_classificationMolecular biologyCell aggregationPoriferaPorifera ; Clathrina clathrus ; lectin ; N-acetyl-glucosamine ; cell aggregation ; proteomicsSponge030104 developmental biologyBiochemistryConcanavalin AProteolysisbiology.proteinCarbohydrate MetabolismFemaleRabbitsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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Clathrin-independent entry of baculovirus triggers uptake of E. coli in non-phagocytic human cells

2008

The prototype baculovirus, Autographa californica multiple nucleopolyhedrovirus, an insect pathogen, holds great potential as a gene therapy vector. To develop transductional targeting and gene delivery by baculovirus, we focused on characterizing the nature and regulation of its uptake in human cancer cells. Baculovirus entered the cells along fluid-phase markers from the raft areas into smooth-surfaced vesicles devoid of clathrin. Notably, regulators associated with macropinocytosis, namely EIPA, Pak1, Rab34, and Rac1, had no significant effect on viral transduction, and the virus did not induce fluid-phase uptake. The internalization and nuclear uptake was, however, affected by mutants o…

RHOASciencevirusesmedia_common.quotation_subjecteducationGene deliveryClathrinCell LineMembrane Lipids03 medical and health sciencesPhagocytosisCell Biology/Membranes and SortingViral entryVirologyEscherichia coliBiochemistry/Cell Signaling and Trafficking StructuresHumansInternalization030304 developmental biologymedia_commonAdenosine Triphosphatases0303 health sciencesMultidisciplinaryBase SequencebiologyADP-Ribosylation FactorsQ030302 biochemistry & molecular biologyHEK 293 cellsRTransfectionMolecular biologyClathrinEndocytosisNucleopolyhedroviruses3. Good healthCell biologyvirologiaADP-Ribosylation Factor 6Cell culturebiology.proteinMedicineRNA InterferenceResearch Article
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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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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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Protein Kinase C-dependent Ubiquitination and Clathrin-mediated Endocytosis of the Cationic Amino Acid Transporter CAT-1*

2011

Cationic amino acid transporter 1 (CAT-1) is responsible for the bulk of the uptake of cationic amino acids in most mammalian cells. Activation of protein kinase C (PKC) leads to down-regulation of the cell surface CAT-1. To examine the mechanisms of PKC-induced down-regulation of CAT-1, a functional mutant of CAT-1 (CAT-1-HA-GFP) was generated in which a hemagglutinin antigen (HA) epitope tag was introduced into the second extracellular loop and GFP was attached to the carboxyl terminus. CAT-1-HA-GFP was stably expressed in porcine aorthic endothelial and human epithelial kidney (HEK) 293 cells. Using the HA antibody internalization assay we have demonstrated that PKC-dependent endocytosis…

Swinemedia_common.quotation_subjectNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesUbiquitin-conjugating enzymeEndocytosisBiochemistryClathrinProtein Structure SecondaryMembrane BiologyAnimalsHumansAmino acid transporterInternalizationMolecular BiologyProtein kinase CProtein Kinase Cmedia_commonCationic Amino Acid Transporter 1biologyEndosomal Sorting Complexes Required for TransportUbiquitinationClathrin-Coated VesiclesCell BiologyReceptor-mediated endocytosisClathrinEndocytosisCell biologyUbiquitin ligaseHEK293 CellsBiochemistrybiology.protein
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Bradykinin-induced Internalization of the Human B2Receptor Requires Phosphorylation of Three Serine and Two Threonine Residues at Its Carboxyl Tail

1999

The binding of bradykinin (BK) to B2 receptor triggers the internalization of the agonist-receptor complex. To investigate the mechanisms and the receptor structures involved in this fundamental process of receptor regulation, the human B2 receptor was mutated within its cytoplasmic tail by complementary strategies of truncation, deletion, and amino acid substitution. Ligand binding, signal transduction, internalization as well as phosphorylation were studied for the mutated receptors expressed in COS, CHO, and HEK 293 cells. Truncation of 44 out of 55 amino acid residues of the receptor's cytoplasmic tail corresponding to positions 321-364 did not alter the kinetics of BK binding and the r…

ThreonineReceptor Bradykinin B2media_common.quotation_subjectMolecular Sequence DataCHO CellsBiologyBradykininTransfectionBiochemistryCell LineSerineCricetinaeSerineAnimalsHumans5-HT5A receptorAmino Acid SequencePhosphorylationInternalizationReceptorMolecular BiologyPeptide sequenceDNA Primersmedia_commonBase SequenceReceptors BradykininCoated Pits Cell-MembraneCell BiologyInterleukin-13 receptorClathrinEndocytosisRecombinant ProteinsCell biologyKineticsBiochemistryCOS CellsPhosphorylationSignal transductionJournal of Biological Chemistry
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A Raft-derived, Pak1-regulated Entry Participates in α2β1 Integrin-dependent Sorting to Caveosomes

2008

We have previously shown that a human picornavirus echovirus 1 (EV1) is transported to caveosomes during 2 h together with its receptor alpha2beta1 integrin. Here, we show that the majority of early uptake does not occur through caveolae. alpha2beta1 integrin, clustered by antibodies or by EV1 binding, is initially internalized from lipid rafts into tubulovesicular structures. These vesicles accumulate fluid-phase markers but do not initially colocalize with caveolin-1 or internalized simian virus 40 (SV40). Furthermore, the internalized endosomes do not contain glycosylphosphatidylinositol (GPI)-anchored proteins or flotillin 1, suggesting that clustered alpha2beta1 integrin does not enter…

Time FactorsEndosomeAntigens Polyomavirus TransformingIntegrinCaveolaeClathrinCaveolinsModels BiologicalAmilorideMembrane MicrodomainsCaveolaeCell Line TumorCaveolinHumansMolecular BiologyDynaminMicroscopy ConfocalbiologyCell BiologyArticlesClathrinCell biologyEnterovirus B HumanIntegrin alpha Mp21-Activated KinasesType C Phospholipasesbiology.proteinIntegrin beta 6Integrin alpha2beta1
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Interactions of silica nanoparticles with lung epithelial cells and the association to flotillins

2012

Amorphous silica nanoparticles (aSNPs) gain increasing popularity for industrial and therapeutic claims. The lung with its surface area of 100-140 m(2) displays an ideal target for therapeutic approaches, but it represents also a serious area of attack for harmful nanomaterials. The exact nature of the cytotoxic effects of NPs is still unknown. Furthermore, cellular pathways and the destiny of internalized NPs are still poorly understood. Therefore, we examined the cytotoxicity (MTS, LDH) and inflammatory responses (IL-8) for different-sized aSNPs (30, 70, 300 nm) on our lung epithelial cells line NCI H441 and endothelial cell line ISO-HAS-1. Additionally, colocalization studies have been c…

Time FactorsEndosomeCell SurvivalHealth Toxicology and MutagenesisEndothelial cellsCytotoxicityEndosomessilica nanoparticlesToxicologyEndocytosisTransfectionClathrinFlotillin-1siliciumFlotillin-2Alveolar-capillary barrierCell Line TumorAlveolar capillary barrierHumansInterleukin 8Inorganic CompoundsParticle SizeCytotoxicityLungbiologyDose-Response Relationship DrugL-Lactate DehydrogenaseInterleukin-8Membrane ProteinsInflammatory responseEpithelial CellsGeneral MedicineTransfectionSilicon DioxideEndocytosisCell biologyLung epithelial cellsEndothelial stem cellEndocytic vesiclebiology.proteinNanoparticlesRNA InterferenceInflammation Mediators
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