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  2. Johannes Gutenberg-Universität Mainz
  3. DFG-491381577-H
Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9226
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dc.contributor.authorLinnert, Joshua-
dc.contributor.authorGüler, Baran E.-
dc.contributor.authorKrzysko, Jacek-
dc.contributor.authorWolfrum, Uwe-
dc.date.accessioned2023-06-26T10:24:30Z-
dc.date.available2023-06-26T10:24:30Z-
dc.date.issued2023-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/9243-
dc.description.abstractVLGR1/ADGRV1 (very large G protein-coupled receptor-1) is the largest known adhesion G protein-coupled receptor. Mutations in VLGR1/ADGRV1 cause Usher syndrome (USH), the most common form of hereditary deaf-blindness, and have been additionally linked to epilepsy. Although VLGR1/ADGRV1 is almost ubiquitously expressed, little is known about the subcellular function and signalling of the VLGR1 protein and thus about mechanisms underlying the development of diseases. Using affinity proteomics, we identified key components of autophagosomes as putative interacting proteins of VLGR1. In addition, whole transcriptome sequencing of the retinae of the Vlgr1/del7TM mouse model revealed altered expression profiles of gene-related autophagy. Monitoring autophagy by immunoblotting and immunocytochemistry of the LC3 and p62 as autophagy marker proteins revealed evoked autophagy in VLGR1-deficient hTERT-RPE1 cells and USH2C patient-derived fibroblasts. Our data demonstrate the molecular and functional interaction of VLGR1 with key components of the autophagy process and point to an essential role of VLGR1 in the regulation of autophagy at internal membranes. The close association of VLGR1 with autophagy helps to explain the pathomechanisms underlying human USH and epilepsy related to VLGR1 defects.en_GB
dc.language.isoengde
dc.rightsCC BY-NC*
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/*
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleThe adhesion G protein-coupled receptor VLGR1/ADGRV1 controls autophagyen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-9226-
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 10 Biologiede
jgu.organisation.number7970-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleBasic & clinical pharmacology & toxicologyde
jgu.journal.volumeVersion of Record (VoR)de
jgu.publisher.year2023-
jgu.publisher.nameWiley-Blackwellde
jgu.publisher.placeOxfordde
jgu.publisher.issn1742-7835de
jgu.organisation.placeMainz-
jgu.subject.ddccode570de
dc.date.updated2023-06-07T07:53:55Z-
jgu.publisher.licenceCC BY-NC-
jgu.publisher.doi10.1111/bcpt.13869de
elements.object.id155919-
elements.object.labelsadhesion GPCR-
elements.object.labelsaffinity proteomics-
elements.object.labelsautophagy-
elements.object.labelsproteostasis-
elements.object.labelsusher syndrome-
elements.object.labelsadhesion GPCR-
elements.object.labelsaffinity proteomics-
elements.object.labelsautophagy-
elements.object.labelsproteostasis-
elements.object.labelsusher syndrome-
elements.object.labels1115 Pharmacology and Pharmaceutical Sciences-
elements.object.labelsPharmacology & Pharmacy-
elements.object.labels3214 Pharmacology and pharmaceutical sciences-
elements.object.typejournal-article-
jgu.organisation.rorhttps://ror.org/023b0x485-
Appears in collections:DFG-491381577-H

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