Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-7074
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dc.contributor.authorKnapp, Barbara-
dc.contributor.authorRoedig, Jens-
dc.contributor.authorBoldt, Karsten-
dc.contributor.authorKrzysko, Jacek-
dc.contributor.authorHorn, Nicola-
dc.contributor.authorUeffing, Marius-
dc.contributor.authorWolfrum, Uwe-
dc.date.accessioned2022-06-02T09:25:42Z-
dc.date.available2022-06-02T09:25:42Z-
dc.date.issued2019-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/7088-
dc.description.abstractAdhesion G protein–coupled receptors (ADGRs) have recently become a target of intense research. Their unique protein structure, which consists of a G protein–coupled receptor combined with long adhesive extracellular domains, suggests a dual role in cell signaling and adhesion. Despite considerable progress in the understanding of ADGR signaling over the past years, the knowledge about ADGR protein networks is still limited. For most receptors, only a few interaction partners are known thus far. We aimed to identify novel ADGR-interacting partners to shed light on cellular protein networks that rely on ADGR function. For this, we applied affinity proteomics, utilizing tandem affinity purifications combined with mass spectrometry. Analysis of the acquired proteomics data provides evidence that ADGRs not only have functional roles at synapses but also at intracellular membranes, namely at the endoplasmic reticulum, the Golgi apparatus, mitochondria, and mitochondria-associated membranes (MAMs). Specifically, we found an association of ADGRs with several scaffold proteins of the membrane-associated guanylate kinases family, elementary units of the γ-secretase complex, the outer/inner mitochondrial membrane, MAMs, and regulators of the Wnt signaling pathways. Furthermore, the nuclear localization of ADGR domains together with their physical interaction with nuclear proteins and several transcription factors suggests a role of ADGRs in gene regulation.en_GB
dc.language.isoengde
dc.rightsCC BY*
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/*
dc.subject.ddc570 Biowissenschaftende_DE
dc.subject.ddc570 Life sciencesen_GB
dc.titleAffinity proteomics identifies novel functional modules related to adhesion GPCRsen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-7074-
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.titleAnnals of the New York Academy of Sciencesde
jgu.journal.volume1456de
jgu.journal.issue1de
jgu.pages.start144de
jgu.pages.end167de
jgu.publisher.year2019-
jgu.publisher.nameWiley-Blackwellde
jgu.publisher.placeOxford u.ade
jgu.publisher.issn1749-6632de
jgu.organisation.placeMainz-
jgu.subject.ddccode570de
jgu.publisher.doi10.1111/nyas.14220de
jgu.organisation.rorhttps://ror.org/023b0x485
Appears in collections:JGU-Publikationen

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