E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses

The innate immune response to many RNA viruses depends on recognition of viral RNA by RIG-I. Here the authors show that, upon virus infection, FBXW7 interacts with RIG-I and inhibits ubiquitin-mediated degradation of RIG-I, resulting in increased interferon signallingin vitro and in vivo.

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Autores principales:	Yinjing Song, Lihua Lai, Zhenlu Chong, Jia He, Yuanyuan Zhang, Yue Xue, Yiwei Xie, Songchang Chen, Ping Dong, Luoquan Chen, Zhimin Chen, Feng Dai, Xiaopeng Wan, Peng Xiao, Xuetao Cao, Yang Liu, Qingqing Wang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8765fcc5c19d48e4bc6d4b98a7ddcbe5
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spelling	oai:doaj.org-article:8765fcc5c19d48e4bc6d4b98a7ddcbe52021-12-02T17:01:18ZE3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses10.1038/ncomms146542041-1723https://doaj.org/article/8765fcc5c19d48e4bc6d4b98a7ddcbe52017-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms14654https://doaj.org/toc/2041-1723The innate immune response to many RNA viruses depends on recognition of viral RNA by RIG-I. Here the authors show that, upon virus infection, FBXW7 interacts with RIG-I and inhibits ubiquitin-mediated degradation of RIG-I, resulting in increased interferon signallingin vitro and in vivo.Yinjing SongLihua LaiZhenlu ChongJia HeYuanyuan ZhangYue XueYiwei XieSongchang ChenPing DongLuoquan ChenZhimin ChenFeng DaiXiaopeng WanPeng XiaoXuetao CaoYang LiuQingqing WangNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yinjing Song Lihua Lai Zhenlu Chong Jia He Yuanyuan Zhang Yue Xue Yiwei Xie Songchang Chen Ping Dong Luoquan Chen Zhimin Chen Feng Dai Xiaopeng Wan Peng Xiao Xuetao Cao Yang Liu Qingqing Wang E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
description	The innate immune response to many RNA viruses depends on recognition of viral RNA by RIG-I. Here the authors show that, upon virus infection, FBXW7 interacts with RIG-I and inhibits ubiquitin-mediated degradation of RIG-I, resulting in increased interferon signallingin vitro and in vivo.
format	article
author	Yinjing Song Lihua Lai Zhenlu Chong Jia He Yuanyuan Zhang Yue Xue Yiwei Xie Songchang Chen Ping Dong Luoquan Chen Zhimin Chen Feng Dai Xiaopeng Wan Peng Xiao Xuetao Cao Yang Liu Qingqing Wang
author_facet	Yinjing Song Lihua Lai Zhenlu Chong Jia He Yuanyuan Zhang Yue Xue Yiwei Xie Songchang Chen Ping Dong Luoquan Chen Zhimin Chen Feng Dai Xiaopeng Wan Peng Xiao Xuetao Cao Yang Liu Qingqing Wang
author_sort	Yinjing Song
title	E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
title_short	E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
title_full	E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
title_fullStr	E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
title_full_unstemmed	E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
title_sort	e3 ligase fbxw7 is critical for rig-i stabilization during antiviral responses
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/8765fcc5c19d48e4bc6d4b98a7ddcbe5
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E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses

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