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Article

Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1

by
Barbara Knapp
1,
Jens Roedig
1,
Heiko Roedig
1,
Jacek Krzysko
1,
Nicola Horn
2,
Baran E. Güler
1,
Deva Krupakar Kusuluri
1,
Adem Yildirim
1,
Karsten Boldt
2,
Marius Ueffing
2,
Ines Liebscher
3 and
Uwe Wolfrum
1,*
1
Institute of Molecular Physiology (ImP), Molecular Cell Biology, Johannes Gutenberg University Mainz, 55128 Mainz, Germany
2
Core Facility for Medical Bioanalytics, Institute for Ophthalmic Research, University of Tuebingen, 72076 Tuebingen, Germany
3
Rudolf Schönheimer Institute of Biochemistry, Faculty of Medicine, Leipzig University, 04103 Leipzig, Germany
*
Author to whom correspondence should be addressed.
Molecules 2022, 27(10), 3108; https://doi.org/10.3390/molecules27103108
Submission received: 16 March 2022 / Revised: 5 May 2022 / Accepted: 6 May 2022 / Published: 12 May 2022
(This article belongs to the Special Issue Molecular Modeling, Synthesis, and Functional Characterization of GPCR (G-Protein Coupled Receptor) Ligands)
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Abstract

The very large G-protein-coupled receptor 1 (VLGR1/ADGRV1) is the largest member of the adhesion G-protein-coupled receptor (ADGR) family. Mutations in VLGR1/ADGRV1 cause human Usher syndrome (USH), a form of hereditary deaf-blindness, and have been additionally linked to epilepsy. In the absence of tangible knowledge of the molecular function and signaling of VLGR1, the pathomechanisms underlying the development of these diseases are still unknown. Our study aimed to identify novel, previously unknown protein networks associated with VLGR1 in order to describe new functional cellular modules of this receptor. Using affinity proteomics, we have identified numerous new potential binding partners and ligands of VLGR1. Tandem affinity purification hits were functionally grouped based on their Gene Ontology terms and associated with functional cellular modules indicative of functions of VLGR1 in transcriptional regulation, splicing, cell cycle regulation, ciliogenesis, cell adhesion, neuronal development, and retinal maintenance. In addition, we validated the identified protein interactions and pathways in vitro and in situ. Our data provided new insights into possible functions of VLGR1, related to the development of USH and epilepsy, and also suggest a possible role in the development of other neuronal diseases such as Alzheimer’s disease.
Keywords: adhesions GPCR; Usher syndrome; affinity proteomics; protein networks adhesions GPCR; Usher syndrome; affinity proteomics; protein networks

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MDPI and ACS Style

Knapp, B.; Roedig, J.; Roedig, H.; Krzysko, J.; Horn, N.; Güler, B.E.; Kusuluri, D.K.; Yildirim, A.; Boldt, K.; Ueffing, M.; et al. Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1. Molecules 2022, 27, 3108. https://doi.org/10.3390/molecules27103108

AMA Style

Knapp B, Roedig J, Roedig H, Krzysko J, Horn N, Güler BE, Kusuluri DK, Yildirim A, Boldt K, Ueffing M, et al. Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1. Molecules. 2022; 27(10):3108. https://doi.org/10.3390/molecules27103108

Chicago/Turabian Style

Knapp, Barbara, Jens Roedig, Heiko Roedig, Jacek Krzysko, Nicola Horn, Baran E. Güler, Deva Krupakar Kusuluri, Adem Yildirim, Karsten Boldt, Marius Ueffing, and et al. 2022. "Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1" Molecules 27, no. 10: 3108. https://doi.org/10.3390/molecules27103108

APA Style

Knapp, B., Roedig, J., Roedig, H., Krzysko, J., Horn, N., Güler, B. E., Kusuluri, D. K., Yildirim, A., Boldt, K., Ueffing, M., Liebscher, I., & Wolfrum, U. (2022). Affinity Proteomics Identifies Interaction Partners and Defines Novel Insights into the Function of the Adhesion GPCR VLGR1/ADGRV1. Molecules, 27(10), 3108. https://doi.org/10.3390/molecules27103108

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