Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex
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...
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| Veröffentlicht in: | Science advances 2022-09, Vol.8 (35), p.eabo7761-eabo7761 |
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| creator | Bous, Julien Fouillen, Aurélien Orcel, Hélène Trapani, Stefano Cong, Xiaojing Fontanel, Simon Saint-Paul, Julie Lai-Kee-Him, Joséphine Urbach, Serge Sibille, Nathalie Sounier, Rémy Granier, Sébastien Mouillac, Bernard Bron, Patrick |
| description | 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. |
| doi_str_mv | 10.1126/sciadv.abo7761 |
| format | Article |
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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. 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| subjects | Biochemistry, Molecular Biology Biomedicine and Life Sciences Life Sciences SciAdv r-articles Structural Biology |
| title | Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex |
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