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Structure of the va...
Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex
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- Bous, J (author)
- Karolinska Institutet
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Fouillen, A (author)
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Orcel, H (author)
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Trapani, S (author)
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Cong, XJ (author)
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Fontanel, S (author)
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Saint-Paul, J (author)
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Lai-Kee-Him, J (author)
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Urbach, S (author)
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Sibille, N (author)
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Sounier, R (author)
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Granier, S (author)
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Mouillac, B (author)
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Bron, P (author)
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(creator_code:org_t)
- American Association for the Advancement of Science (AAAS), 2022
- 2022
- English.
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In: Science advances. - : American Association for the Advancement of Science (AAAS). - 2375-2548. ; 8:35, s. eabo7761-
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https://doi.org/10.1...
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Abstract
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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.
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- ref (subject category)
- art (subject category)
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To the university's database
- By the author/editor
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Bous, J
-
Fouillen, A
-
Orcel, H
-
Trapani, S
-
Cong, XJ
-
Fontanel, S
-
show more...
-
Saint-Paul, J
-
Lai-Kee-Him, J
-
Urbach, S
-
Sibille, N
-
Sounier, R
-
Granier, S
-
Mouillac, B
-
Bron, P
-
show less...
- Articles in the publication
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Science advances
- By the university
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Karolinska Institutet