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Article Dans Une Revue Science Advances Année : 2022

Structure of the vasopressin hormone–V2 receptor–β-arrestin1 ternary complex

Hélène Orcel
Xiaojing Cong
Simon Fontanel
Julie Saint-Paul
Serge Urbach
Rémy Sounier

Résumé

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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Dates et versions

hal-03790728 , version 1 (04-10-2022)

Identifiants

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Julien Bous, Aurélien Fouillen, Hélène Orcel, Stefano Trapani, Xiaojing Cong, et al.. Structure of the vasopressin hormone–V2 receptor–β-arrestin1 ternary complex. Science Advances , 2022, 8 (35), pp.eabo7761. ⟨10.1126/sciadv.abo7761⟩. ⟨hal-03790728⟩
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