Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-7074
Authors: Knapp, Barbara
Roedig, Jens
Boldt, Karsten
Krzysko, Jacek
Horn, Nicola
Ueffing, Marius
Wolfrum, Uwe
Title: Affinity proteomics identifies novel functional modules related to adhesion GPCRs
Online publication date: 2-Jun-2022
Language: english
Abstract: Adhesion 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.
DDC: 570 Biowissenschaften
570 Life sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 10 Biologie
Place: Mainz
ROR: https://ror.org/023b0x485
DOI: http://doi.org/10.25358/openscience-7074
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC BY
Information on rights of use: https://creativecommons.org/licenses/by/4.0/
Journal: Annals of the New York Academy of Sciences
1456
1
Pages or article number: 144
167
Publisher: Wiley-Blackwell
Publisher place: Oxford u.a
Issue date: 2019
ISSN: 1749-6632
Publisher DOI: 10.1111/nyas.14220
Appears in collections:JGU-Publikationen

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