Search results for "Vesicular Transport Protein"

showing 10 items of 40 documents

Recessive mutations in EPG5 cause Vici syndrome, a multisystem disorder with defective autophagy

2013

Vici syndrome is a recessively inherited multisystem disorder characterized by callosal agenesis, cataracts, cardiomyopathy, combined immunodeficiency and hypopigmentation. To investigate the molecular basis of Vici syndrome, we carried out exome and Sanger sequence analysis in a cohort of 18 affected individuals. We identified recessive mutations in EPG5 (previously KIAA1632), indicating a causative role in Vici syndrome. EPG5 is the human homolog of the metazoan-specific autophagy gene epg-5, encoding a key autophagy regulator (ectopic P-granules autophagy protein 5) implicated in the formation of autolysosomes. Further studies showed a severe block in autophagosomal clearance in muscle a…

BiopsyVesicular Transport ProteinsAutophagy-Related ProteinsGenes RecessiveConsanguinityBiologymedicine.disease_causeArticleCataract03 medical and health sciencesConsanguinity0302 clinical medicineCataractsAntigens NeoplasmGeneticsmedicineAutophagyHumansVici syndromeExomeFamilyMuscle SkeletalExomeImmunodeficiency030304 developmental biologyGenetics0303 health sciencesMutationAutophagyIntracellular Signaling Peptides and ProteinsLysosome-Associated Membrane GlycoproteinsProteinsmedicine.diseaseMutationAutophagy Protein 5Agenesis of Corpus CallosumLysosomes030217 neurology & neurosurgeryNature genetics
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Soluble N-ethylmaleimide-sensitive-factor attachment protein and N-ethylmaleimide-insensitive factors are required for Ca2+-stimulated exocytosis of …

1996

Ca2+ stimulates exocytosis in permeabilized insulin-secreting cells. To investigate the putative cytosolic components involved in the Ca2+ response, HIT-T15 cells (a pancreatic B-cell line) were permeabilized with streptolysin-O, a procedure that allows rapid exchange of soluble components including macromolecules. We found that in this cell preparation the secretory response to Ca2+ but not to guanosine 5'-[gamma-thio]triphosphate was lost as a function of time and could be restored by rat brain cytosol in a concentration-dependent manner. Reconstitutive activity of rat brain cytosol was found in a high-molecular-mass heat-labile partially N-ethylmaleimide(NEM)-sensitive fraction. The NEM-…

Cell Membrane Permeabilitymedicine.medical_treatmentBlotting WesternVesicular Transport ProteinsGuanosineBiologyBiochemistryExocytosisExocytosislaw.inventionCell Linechemistry.chemical_compoundIslets of LangerhansCytosolBacterial ProteinslawInsulin SecretionmedicineAnimalsInsulinheterocyclic compoundsAttachment proteinMolecular BiologyN-Ethylmaleimide-Sensitive ProteinsBrain ChemistryInsulinN-EthylmaleimideMembrane ProteinsCell BiologyRecombinant ProteinsCell biologyRatsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsCytosolchemistryEthylmaleimideGuanosine 5'-O-(3-Thiotriphosphate)StreptolysinsRecombinant DNACalciumSoluble NSF attachment proteinCarrier ProteinsResearch ArticleThe Biochemical journal
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Characterization of the transporterB0AT3 (Slc6a17) in the rodent central nervous system.

2013

Abstract Background The vesicular B0AT3 transporter (SLC6A17), one of the members of the SLC6 family, is a transporter for neutral amino acids and is exclusively expressed in brain. Here we provide a comprehensive expression profile of B0AT3 in mouse brain using in situ hybridization and immunohistochemistry. Results We confirmed previous expression data from rat brain and used a novel custom made antibody to obtain detailed co-labelling with several cell type specific markers. B0AT3 was highly expressed in both inhibitory and excitatory neurons. The B0AT3 expression was highly overlapping with those of vesicular glutamate transporter 2 (VGLUT2) and vesicular glutamate transporter 1 (VGLUT1…

Central Nervous SystemMaleSerotonin reuptake inhibitorVesicular glutamate transporter 1Central nervous systemVesicular Transport ProteinsNerve Tissue ProteinsIn situ hybridizationPharmacology and ToxicologyPharmacologyBiologyPlasma Membrane Neurotransmitter Transport ProteinsRats Sprague-DawleyCellular and Molecular NeuroscienceGlutamatergicMiceDopaminePregnancyMonoaminergicmedicineAnimalsRats WistarCells CulturedNeuronsGeneral NeuroscienceNeurosciencesTransporterFarmakologi och toxikologiEmbryo MammalianAntidepressive AgentsRatsMice Inbred C57BLProtein Transportmedicine.anatomical_structureGene Expression Regulationbiology.proteinFemaleFood DeprivationNeurovetenskapermedicine.drugResearch ArticleBMC neuroscience
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Competitive binding of Rab21 and p120RasGAP to integrins regulates receptor traffic and migration

2011

P120RasGAP competes with Rab21 for binding to the cytoplasmic domain of integrin α-subunits, thereby promoting receptor escape from early endosomes and recycling to the plasma membrane.

CytoplasmIntegrinsEndosomeEndocytic cycleIntegrinVesicular Transport ProteinsEndosomesCD49cBinding CompetitiveModels BiologicalArticleCollagen receptor03 medical and health sciencesMice0302 clinical medicineSDG 3 - Good Health and Well-beingCell MovementCell Line TumorAnimalsHumansResearch Articles030304 developmental biology0303 health sciencesbiologyCell Membranep120 GTPase Activating ProteinCell BiologyCell biologyProtein Structure TertiaryIntegrin alpha Mrab GTP-Binding Proteins030220 oncology & carcinogenesisbiology.protein/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6RabProtein Binding
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The Co‐mutational Spectrum Determines the Therapeutic Response in Murine FGFR2 Fusion‐Driven Cholangiocarcinoma

2021

Background and aims Intrahepatic cholangiocarcinoma (ICC) is the second most common primary liver cancer and a highly lethal malignancy. Chemotherapeutic options are limited, but a considerable subset of patients harbors genetic lesions for which targeted agents exist. Fibroblast growth factor receptor 2 (FGFR2) fusions belong to the most frequent and therapeutically relevant alterations in ICC, and the first FGFR inhibitor was recently approved for the treatment of patients with progressed, fusion-positive ICC. Response rates of up to 35% indicate that FGFR-targeted therapies are beneficial in many but not all patients. Thus far, no established biomarkers exist that predict resistance or r…

Fetal Proteins0301 basic medicineAntimetabolites AntineoplasticCombination therapymedicine.medical_treatmentFGFR InhibitionVesicular Transport ProteinsCyclic AMP Response Element-Binding Protein Amedicine.disease_causeDeoxycytidineMalignant transformationTargeted therapyCholangiocarcinomaProto-Oncogene Proteins p21(ras)Mice03 medical and health sciencesLiver Neoplasms Experimental0302 clinical medicineAntigens NeoplasmmedicineAnimalsReceptor Fibroblast Growth Factor Type 2Protein Kinase InhibitorsCell ProliferationHepatologyOncogenebusiness.industryFibroblast growth factor receptor 2AdenosylhomocysteinasePhenylurea CompoundsGemcitabineBile Ducts IntrahepaticCell Transformation NeoplasticPyrimidines030104 developmental biologyBile Duct NeoplasmsFibroblast growth factor receptorMutationCancer research030211 gastroenterology & hepatologyKRASGene FusionbusinessCo-Repressor ProteinsMicrotubule-Associated ProteinsHepatology
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Mapping the protein composition oftrans-Golgi network (TGN)-derived carrier vesicles from polarized MDCK cells

1998

In polarized MDCK cells, proteins and lipids are sorted in the trans-Golgi network /TGN) and packaged into different vesicular carriers that are delivered to the apical or basolateral cell surface. To gain insight into the sorting and trafficking machinery, we have previously isolated TGN-derived carrier vesicles from perforated MDCK cells. The composition of immuno-isolated apical and basolateral carriers was mapped by two-dimensional (2-D) gel electrophoresis. Here we describe the identification of several components of the vesicle fraction by using three different methods. 2-D gel comigration was performed with carrier vesicles isolated from metabolically labeled MDCK cells and human epi…

G proteinImmunoblottingMolecular Sequence DataClinical BiochemistryGolgi ApparatusPeptideBiologyPeptide MappingBiochemistryCell LineAnalytical Chemistrysymbols.namesakeDogsmedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceGel electrophoresischemistry.chemical_classificationVesicleCell PolarityProteinsGolgi apparatusCell biologyVesicular transport proteinmedicine.anatomical_structurechemistrysymbolsKeratinocyteAnnexin A2Electrophoresis
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Identification of novel interaction partners for Vlgr1b/GPR98 - a key component of the periciliary Usher syndrome protein network in photoreceptor ce…

2012

The human Usher syndrome (USH) is the most common form of combined hereditary deaf-blindness. Three clinical subtypes (USH1-3) are differentiated based on severity, age of onset and progression of the symptoms. Mutations in the GPR98 gene encoding the USH2C protein Vlgr1b or GPR98 cause USH2, the most common form of USH. The G-protein coupled receptor Vlgr1b was previously identified as a component of the periciliary USH protein network, crucial for ciliary cargo transport in photoreceptors. Nonetheless, the exact role of Vlgr1b in this and other cellular processes remains to be elucidated. To learn more about its involvement in cellular functions we searched for novel interaction partners …

GeneticsTandem affinity purificationRegulation of gene expressionScaffold proteinlcsh:CytologyCiliumCell BiologyComputational biologyBiologymedicine.diseaseInteractomeVesicular transport proteinCiliopathyPoster Presentationmedicinelcsh:QH573-671Transcription factorCilia
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Cohen syndrome is associated with major glycosylation defects

2014

International audience; Cohen syndrome (CS) is a rare autosomal recessive disorder with multisytemic clinical features due to mutations in the VPS13B gene, which has recently been described encoding a mandatory membrane protein involved in Golgi integrity. As the Golgi complex is the place where glycosylation of newly synthesized proteins occurs, we hypothesized that VPS13B deficiency, responsible of Golgi apparatus disturbance, could lead to glycosylation defects and/or mysfunction of this organelle, and thus be a cause of the main clinical manifestations of CS. The glycosylation status of CS serum proteins showed a very unusual pattern of glycosylation characterized by a significant accum…

GlycanGlycosylationGlycosylationEndosomeDevelopmental Disabilities[SDV]Life Sciences [q-bio]Vesicular Transport ProteinsGolgi ApparatusFingers03 medical and health scienceschemistry.chemical_compoundsymbols.namesake0302 clinical medicineAntigens CDIntellectual DisabilityMyopiaGeneticsHumansObesityMolecular BiologyGenetics (clinical)030304 developmental biology0303 health sciencesbiology[ SDV ] Life Sciences [q-bio]Retinal DegenerationTransferrinGeneral MedicineFibroblastsBrefeldin AGolgi apparatusIntercellular Adhesion Molecule-1Cell biologyVPS13BchemistryMembrane proteinBiochemistryMicrocephalysymbolsO-linked glycosylationbiology.proteinMuscle HypotoniaElectrophoresis Polyacrylamide GelRNA InterferenceCell Adhesion Molecules030217 neurology & neurosurgery
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Hepatitis B subviral envelope particles use the COPII machinery for intracellular transport via selective exploitation of Sec24A and Sec23B

2020

Hepatitis B virus (HBV) is a leading cause of liver disease. Its success as a human pathogen is related to the immense production of subviral envelope particles (SVPs) contributing to viral persistence by interfering with immune functions. To explore cellular pathways involved in SVP formation and egress, we investigated host-pathogen interactions. Yeast-based proteomics revealed Sec24A, a component of the coat protein complex II (COPII), as an interaction partner of the HBV envelope S domain. To understand how HBV co-opts COPII as a proviral machinery, we studied roles of key Sec proteins in HBV-expressing liver cells. Silencing of Sar1, Sec23, and Sec24, which promote COPII assembly conco…

Hepatitis B virusImmunology610 MedizinVesicular Transport ProteinsBiologymedicine.disease_causeProteomicsEndoplasmic ReticulumMicrobiologyCell Line03 medical and health sciencesDownregulation and upregulationTranscription (biology)610 Medical sciencesVirologyddc:570medicineGene silencingHumansProtein IsoformsSecretionRNA Small InterferingCOPII030304 developmental biologyHepatitis B virus0303 health sciences030306 microbiologyEndoplasmic reticulumBiological TransportHepatitis Bdiseases infection microbe–cell interaction proteomics virusesCell biologyHost-Pathogen InteractionsHepatocytesCOP-Coated Vesicles
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Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin.

2007

ABSTRACT Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two endocytic host proteins, the ubiquitin-interacting adaptor γ2-adaptin and the Nedd4 ubiquitin ligase. Here, we demonstrate that HBV release also requires the cellular machinery that generates internal vesicles of multivesicular bodies (MVBs). In order to perturb the MVB machinery in HBV-replicating liver cells, we used ectopic expression of dominant-negative mutants of different MVB components, like the ESCRT-III complex-forming CHMP proteins and the Vps4 ATPases. Upon coexpression of mutated CHMP3, CHMP4B, or CHMP4C forms, as well as of ATPa…

Hepatitis B virusVacuolar Proton-Translocating ATPasesEndosomeImmunologyEndocytic cycleVesicular Transport Proteinsmacromolecular substancesEndosomesmedicine.disease_causeMicrobiologyESCRTVirusCell LineViral ProteinsVirologymedicineHumansAdaptor Protein Complex gamma SubunitsHepatitis B virusAdenosine TriphosphatasesMicroscopy ConfocalbiologyEndosomal Sorting Complexes Required for TransportVirus AssemblyDNA virusMolecular biologyUbiquitin ligaseCell biologyGenome Replication and Regulation of Viral Gene ExpressionMicroscopy FluorescenceInsect Sciencebiology.proteinHepatocytesATPases Associated with Diverse Cellular ActivitiesEctopic expressionJournal of virology
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