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- Bous, JKarolinska Institutet (author)
Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex
- Article/chapterEnglish2022
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- American Association for the Advancement of Science (AAAS),2022
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- LIBRIS-ID:oai:prod.swepub.kib.ki.se:151348776
- http://kipublications.ki.se/Default.aspx?queryparsed=id:151348776URI
- https://doi.org/10.1126/sciadv.abo7761DOI
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- Language:English
- Summary in:English
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- Arrestins interact with G protein–coupled receptors (GPCRs) to stop G protein activation and to initiate key signaling pathways. Recent structural studies shed light on the molecular mechanisms involved in GPCR-arrestin coupling, but whether this process is conserved among GPCRs is poorly understood. Here, we report the cryo–electron microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with β-arrestin1. It reveals an atypical position of β-arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/β-arrestin1 interface involving all receptor intracellular loops. Phosphorylated sites of the V2R carboxyl terminus are clearly identified and interact extensively with the β-arrestin1 N-lobe, in agreement with structural data obtained with chimeric or synthetic systems. Overall, these findings highlight a notable structural variability among GPCR-arrestin signaling complexes.
Added entries (persons, corporate bodies, meetings, titles ...)
- Fouillen, A (author)
- Orcel, H (author)
- Trapani, S (author)
- Cong, XJ (author)
- Fontanel, S (author)
- Saint-Paul, J (author)
- Lai-Kee-Him, J (author)
- Urbach, S (author)
- Sibille, N (author)
- Sounier, R (author)
- Granier, S (author)
- Mouillac, B (author)
- Bron, P (author)
- Karolinska Institutet (creator_code:org_t)
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- In:Science advances: American Association for the Advancement of Science (AAAS)8:35, s. eabo7761-2375-2548
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