Nature Communications (Apr 2021)
Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
- 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
Affiliations
- Qing-Tao He
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Peng Xiao
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Shen-Ming Huang
- Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Peking University
- Ying-Li Jia
- Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Peking University
- Zhong-Liang Zhu
- School of Life Sciences, University of Science and Technology of China
- Jing-Yu Lin
- Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Peking University
- Fan Yang
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Xiao-Na Tao
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Ru-Jia Zhao
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Feng-Yuan Gao
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Xiao-Gang Niu
- Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, School of Life Sciences, Peking University
- Kun-Hong Xiao
- Department of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh
- Jiangyun Wang
- Institute of Biophysics, Chinese Academy of Sciences
- Changwen Jin
- Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, School of Life Sciences, Peking University
- Jin-Peng Sun
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- Xiao Yu
- Key Laboratory Experimental Teratology of the Ministry of Education and Department of Physiology, School of Basic Medical Sciences, Cheeloo college of Medicine, Shandong University
- DOI
- https://doi.org/10.1038/s41467-021-22731-x
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 16
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.
