Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis

RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.

Bibliographic Details
Main Authors:	Xixi Zhang, Haiwei Zhang, Chengxian Xu, Xiaoming Li, Ming Li, Xiaoxia Wu, Wenjuan Pu, Bin Zhou, Haikun Wang, Dali Li, Qiurong Ding, Hao Ying, Hui Wang, Haibing Zhang
Format:	Article
Language:	English
Published:	Nature Publishing Group 2019-09-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-019-11839-w

id	doaj-7a20ff8bd8654fe78c8cee847d1dc433
record_format	Article
spelling	doaj-7a20ff8bd8654fe78c8cee847d1dc4332021-05-11T11:55:28ZengNature Publishing GroupNature Communications2041-17232019-09-0110111510.1038/s41467-019-11839-wUbiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesisXixi Zhang0Haiwei Zhang1Chengxian Xu2Xiaoming Li3Ming Li4Xiaoxia Wu5Wenjuan Pu6Bin Zhou7Haikun Wang8Dali Li9Qiurong Ding10Hao Ying11Hui Wang12Haibing Zhang13CAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesThe State Key Laboratory of Cell Biology, CAS Center for Excellence on Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of SciencesThe State Key Laboratory of Cell Biology, CAS Center for Excellence on Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of SciencesKey Laboratory of Molecular Virology and Immunology, Unit of the Regulation of Immune Cell Differentiation, Institute Pasteur of Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of SciencesShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University (ECNU)CAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesCAS Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesRIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.https://doi.org/10.1038/s41467-019-11839-w
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Xixi Zhang Haiwei Zhang Chengxian Xu Xiaoming Li Ming Li Xiaoxia Wu Wenjuan Pu Bin Zhou Haikun Wang Dali Li Qiurong Ding Hao Ying Hui Wang Haibing Zhang
spellingShingle	Xixi Zhang Haiwei Zhang Chengxian Xu Xiaoming Li Ming Li Xiaoxia Wu Wenjuan Pu Bin Zhou Haikun Wang Dali Li Qiurong Ding Hao Ying Hui Wang Haibing Zhang Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis Nature Communications
author_facet	Xixi Zhang Haiwei Zhang Chengxian Xu Xiaoming Li Ming Li Xiaoxia Wu Wenjuan Pu Bin Zhou Haikun Wang Dali Li Qiurong Ding Hao Ying Hui Wang Haibing Zhang
author_sort	Xixi Zhang
title	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_short	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_full	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_fullStr	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_full_unstemmed	Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis
title_sort	ubiquitination of ripk1 suppresses programmed cell death by regulating ripk1 kinase activation during embryogenesis
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2019-09-01
description	RIPK1 integrates signals that drive both NF-κB activation and cell death pathways. Here Zhang et al. generate RIPK1 knock-in mice lacking a major ubiquitination site and demonstrate that this modification is important to suppress cell death during embryogenesis and inflammation postnatally.
url	https://doi.org/10.1038/s41467-019-11839-w
work_keys_str_mv	AT xixizhang ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT haiweizhang ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT chengxianxu ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT xiaomingli ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT mingli ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT xiaoxiawu ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT wenjuanpu ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT binzhou ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT haikunwang ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT dalili ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT qiurongding ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT haoying ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT huiwang ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis AT haibingzhang ubiquitinationofripk1suppressesprogrammedcelldeathbyregulatingripk1kinaseactivationduringembryogenesis
_version_	1721445742295384064

Ubiquitination of RIPK1 suppresses programmed cell death by regulating RIPK1 kinase activation during embryogenesis

Similar Items