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

Authors :
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
Source :
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Publication Year :
2021
Publisher :
Nature Portfolio, 2021.

Abstract

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.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
12
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.5ffe1d9ce0c04791b889a4c6d158110f
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-021-22731-x