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Article

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

Nature communications - 11 Dec 2020

Li Xingyan, Zhang Mengmeng, Huang Xinyue, Liang Wei, Li Ganquan, Lu Xiaojuan, Li Yanxia, Pan Heling, Shi Linyu, Zhu Hong, Qian Lihui, Shan Bing, Yuan Junying

Abstract excerpt

RIPK1 is a death-domain (DD) containing kinase involved in regulating apoptosis, necroptosis and inflammation. RIPK1 activation is known to be regulated by its DD-mediated interaction and ubiquitination, though underlying mechanisms remain incompletely understood. Here we show that K627 in human RIPK1-DD and its equivalent K612 in murine RIPK1-DD is a key ubiquitination site that regulates the overall...

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Identifiers

PMID: 33311474
DOI: 10.1038/s41467-020-19935-y
PMCID: PMC7733462

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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