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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5ffe1d9ce0c04791b889a4c6d158110f
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spelling	oai:doaj.org-article:5ffe1d9ce0c04791b889a4c6d158110f2021-12-02T18:28:38ZStructural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-210.1038/s41467-021-22731-x2041-1723https://doaj.org/article/5ffe1d9ce0c04791b889a4c6d158110f2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22731-xhttps://doaj.org/toc/2041-1723The 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.Qing-Tao HePeng XiaoShen-Ming HuangYing-Li JiaZhong-Liang ZhuJing-Yu LinFan YangXiao-Na TaoRu-Jia ZhaoFeng-Yuan GaoXiao-Gang NiuKun-Hong XiaoJiangyun WangChangwen JinJin-Peng SunXiao YuNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
description	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.
format	article
author	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
author_facet	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
author_sort	Qing-Tao He
title	Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
title_short	Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
title_full	Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
title_fullStr	Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
title_full_unstemmed	Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
title_sort	structural studies of phosphorylation-dependent interactions between the v2r receptor and arrestin-2
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5ffe1d9ce0c04791b889a4c6d158110f
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Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2

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