Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2

Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2

The interaction between a GPCR, such as the vasopressin receptor-2 (V2R), and arrestin depends on the receptors’ phosphorylation pattern. Here authors use FRET and NMR to analyze the phosphorylation patterns of the V2R-arrestin complex and show that phospho-interactions are the key determinants of s...

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Autores principales: Qing-Tao He, Peng Xiao, Shen-Ming Huang, Ying-Li Jia, Zhong-Liang Zhu, Jing-Yu Lin, Fan Yang, Xiao-Na Tao, Ru-Jia Zhao, Feng-Yuan Gao, Xiao-Gang Niu, Kun-Hong Xiao, Jiangyun Wang, Changwen Jin, Jin-Peng Sun, Xiao Yu
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/5ffe1d9ce0c04791b889a4c6d158110f
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Sumario:The interaction between a GPCR, such as the vasopressin receptor-2 (V2R), and arrestin depends on the receptors’ phosphorylation pattern. Here authors use FRET and NMR to analyze the phosphorylation patterns of the V2R-arrestin complex and show that phospho-interactions are the key determinants of selective arrestin conformational states and correlated functions.

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