scholarly journals The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Hui Song ◽  
Bingyu Liu ◽  
Wanwan Huai ◽  
Zhongxia Yu ◽  
Wenwen Wang ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Nlrp3 Inflammasome ◽  
E3 Ubiquitin Ligase ◽  
Proteasomal Degradation ◽  
Inflammasome Activation ◽  
Nlrp3 Inflammasome Activation

scholarly journals The E3 Ubiquitin Ligase Tripartite Motif 33 Is Essential for Cytosolic RNA–Induced NLRP3 Inflammasome Activation

2014 ◽  
Vol 193 (7) ◽  
pp. 3676-3682 ◽  
Author(s):  
Leiyun Weng ◽  
Hiroki Mitoma ◽  
Coline Tricot ◽  
Musheng Bao ◽  
Ying Liu ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Nlrp3 Inflammasome ◽  
E3 Ubiquitin Ligase ◽  
Inflammasome Activation ◽  
Nlrp3 Inflammasome Activation ◽  
Tripartite Motif

scholarly journals Sequential ubiquitination of NLRP3 by RNF125 and Cbl-b limits inflammasome activation and endotoxemia

2020 ◽  
Vol 217 (4) ◽  
Author(s):  
Juan Tang ◽  
Sha Tu ◽  
Guoxin Lin ◽  
Hui Guo ◽  
Chengkai Yan ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Lethal Dose ◽  
E3 Ubiquitin Ligase ◽  
Inflammasome Activation ◽  
Dependent Manner ◽  
Leucine Rich Repeat ◽  
Nlrp3 Inflammasome Activation ◽  
Repeat Domain ◽  
Nlrp3 Inflammasomes ◽  
Lrr Domain

Aberrant NLRP3 inflammasome activation contributes to the development of endotoxemia. The importance of negative regulation of NLRP3 inflammasomes remains poorly understood. Here, we show that the E3 ubiquitin ligase Cbl-b is essential for preventing endotoxemia induced by a sub-lethal dose of LPS via a caspase-11/NLRP3–dependent manner. Further studies show that NLRP3 undergoes both K63- and K48-linked polyubiquitination. Cbl-b binds to the K63-ubiquitin chains attached to the NLRP3 leucine-rich repeat domain (LRR) via its ubiquitin-associated region (UBA) and then targets NLRP3 at K496 for K48-linked ubiquitination and proteasome-mediated degradation. We also identify RNF125 as an additional E3 ubiquitin ligase that initiates K63-linked ubiquitination of the NLRP3 LRR domain. Therefore, NLRP3 is sequentially ubiquitinated by K63- and K48-linked ubiquitination, thus keeping the NLRP3 inflammasomes in check and restraining endotoxemia.

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