Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners

RIPK1 is a critical kinase which mediates necroptosis, apoptosis and inflammation. Regulation of RIPK1 by ubiquitination is being intensively investigated. Here, the authors made knock-in RIPK1-K612R mice and demonstrate that this mutation alters the RIPK1 ubiquitinylation pattern and inhibits its p...

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Autores principales:	Xingyan Li, Mengmeng Zhang, Xinyue Huang, Wei Liang, Ganquan Li, Xiaojuan Lu, Yanxia Li, Heling Pan, Linyu Shi, Hong Zhu, Lihui Qian, Bing Shan, Junying Yuan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/13104a8bcb9e4fa4a4030c31c509ba7c
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spelling	oai:doaj.org-article:13104a8bcb9e4fa4a4030c31c509ba7c2021-12-02T14:16:24ZUbiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners10.1038/s41467-020-19935-y2041-1723https://doaj.org/article/13104a8bcb9e4fa4a4030c31c509ba7c2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19935-yhttps://doaj.org/toc/2041-1723RIPK1 is a critical kinase which mediates necroptosis, apoptosis and inflammation. Regulation of RIPK1 by ubiquitination is being intensively investigated. Here, the authors made knock-in RIPK1-K612R mice and demonstrate that this mutation alters the RIPK1 ubiquitinylation pattern and inhibits its prodeath kinase activity in response to TNFα but sensitizes cell death to TLRs signals.Xingyan LiMengmeng ZhangXinyue HuangWei LiangGanquan LiXiaojuan LuYanxia LiHeling PanLinyu ShiHong ZhuLihui QianBing ShanJunying YuanNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-18 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Xingyan Li Mengmeng Zhang Xinyue Huang Wei Liang Ganquan Li Xiaojuan Lu Yanxia Li Heling Pan Linyu Shi Hong Zhu Lihui Qian Bing Shan Junying Yuan Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
description	RIPK1 is a critical kinase which mediates necroptosis, apoptosis and inflammation. Regulation of RIPK1 by ubiquitination is being intensively investigated. Here, the authors made knock-in RIPK1-K612R mice and demonstrate that this mutation alters the RIPK1 ubiquitinylation pattern and inhibits its prodeath kinase activity in response to TNFα but sensitizes cell death to TLRs signals.
format	article
author	Xingyan Li Mengmeng Zhang Xinyue Huang Wei Liang Ganquan Li Xiaojuan Lu Yanxia Li Heling Pan Linyu Shi Hong Zhu Lihui Qian Bing Shan Junying Yuan
author_facet	Xingyan Li Mengmeng Zhang Xinyue Huang Wei Liang Ganquan Li Xiaojuan Lu Yanxia Li Heling Pan Linyu Shi Hong Zhu Lihui Qian Bing Shan Junying Yuan
author_sort	Xingyan Li
title	Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
title_short	Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
title_full	Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
title_fullStr	Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
title_full_unstemmed	Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners
title_sort	ubiquitination of ripk1 regulates its activation mediated by tnfr1 and tlrs signaling in distinct manners
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/13104a8bcb9e4fa4a4030c31c509ba7c
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Ubiquitination of RIPK1 regulates its activation mediated by TNFR1 and TLRs signaling in distinct manners

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