Post-translational control of NLRP3 inflammasome signaling

被引:17
|
作者
O'Keefe, Meghan E. [1 ]
Dubyak, George R. [2 ]
Abbott, Derek W. [1 ]
机构
[1] Case Western Reserve Univ, Sch Med, Dept Pathol, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Cleveland, OH USA
关键词
NF-KAPPA-B; BRUTONS TYROSINE KINASE; NITRIC-OXIDE; CASPASE-1; ACTIVATION; SUBSTRATE MOTIFS; UBIQUITIN LIGASE; GASDERMIN D; PROTEIN; PHOSPHORYLATION; ASC;
D O I
10.1016/j.jbc.2024.107386
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Inflammasomes serve as critical sensors for disruptions to cellular homeostasis, with inflammasome assembly leading to inflammatory caspase activation, gasdermin cleavage, and cytokine release. While the canonical pathways leading to priming, assembly, and pyroptosis are well characterized, recent work has begun to focus on the role of post-translational modifications (PTMs) in regulating inflammasome activity. A diverse array of PTMs, including phosphorylation, ubiquitination, SUMOylation, acetylation, and glycosylation, exert both activating and inhibitory influences on members of the inflammasome cascade through effects on protein-protein interactions, stability, and localization. Dysregulation of inflammasome activation is associated with a number of inflammatory diseases, and evidence is emerging that aberrant modification of inflammasome components contributes to this dysregulation. This review provides insight into PTMs within the NLRP3 inflammasome pathway and their functional consequences on the signaling cascade and highlights outstanding questions that remain regarding the complex web of signals at play.
引用
收藏
页数:15
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