Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR

Upon stimulation by agonist binding, the C-terminal regions of G-protein-coupled receptors (GPCRs) become phosphorylated by GPCR kinases, and phosphorylated GPCRs bind arrestin. Here the authors give structural insights into the phosphorylation induced conformational changes in GPCRs by performing N...

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Autores principales:	Yutaro Shiraishi, Mei Natsume, Yutaka Kofuku, Shunsuke Imai, Kunio Nakata, Toshimi Mizukoshi, Takumi Ueda, Hideo Iwaï, Ichio Shimada
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/11dca4d48ec6418dbf505466ac65a7b4
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spelling	oai:doaj.org-article:11dca4d48ec6418dbf505466ac65a7b42021-12-02T17:31:27ZPhosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR10.1038/s41467-017-02632-82041-1723https://doaj.org/article/11dca4d48ec6418dbf505466ac65a7b42018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02632-8https://doaj.org/toc/2041-1723Upon stimulation by agonist binding, the C-terminal regions of G-protein-coupled receptors (GPCRs) become phosphorylated by GPCR kinases, and phosphorylated GPCRs bind arrestin. Here the authors give structural insights into the phosphorylation induced conformational changes in GPCRs by performing NMR studies with the β2-adrenoceptor.Yutaro ShiraishiMei NatsumeYutaka KofukuShunsuke ImaiKunio NakataToshimi MizukoshiTakumi UedaHideo IwaïIchio ShimadaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yutaro Shiraishi Mei Natsume Yutaka Kofuku Shunsuke Imai Kunio Nakata Toshimi Mizukoshi Takumi Ueda Hideo Iwaï Ichio Shimada Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
description	Upon stimulation by agonist binding, the C-terminal regions of G-protein-coupled receptors (GPCRs) become phosphorylated by GPCR kinases, and phosphorylated GPCRs bind arrestin. Here the authors give structural insights into the phosphorylation induced conformational changes in GPCRs by performing NMR studies with the β2-adrenoceptor.
format	article
author	Yutaro Shiraishi Mei Natsume Yutaka Kofuku Shunsuke Imai Kunio Nakata Toshimi Mizukoshi Takumi Ueda Hideo Iwaï Ichio Shimada
author_facet	Yutaro Shiraishi Mei Natsume Yutaka Kofuku Shunsuke Imai Kunio Nakata Toshimi Mizukoshi Takumi Ueda Hideo Iwaï Ichio Shimada
author_sort	Yutaro Shiraishi
title	Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
title_short	Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
title_full	Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
title_fullStr	Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
title_full_unstemmed	Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR
title_sort	phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by nmr
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/11dca4d48ec6418dbf505466ac65a7b4
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Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR

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