PDF(Pubmed)
Abstract：
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.
摘要：
炎性体作为破坏细胞稳态的关键传感器，炎症小体组装导致炎性半胱天冬酶激活，gasdermin裂解，和细胞因子释放。虽然导致启动的典型途径，装配,焦亡的特征很好，最近的工作已经开始关注翻译后修饰（PTM）在调节炎性体活性中的作用。各种各样的PTM，包括磷酸化，泛素化，SUMOylation,乙酰化,和糖基化，通过对蛋白质-蛋白质相互作用的影响对炎性小体级联的成员施加激活和抑制影响，稳定性,和本地化。炎症小体激活的失调与许多炎症性疾病有关。并且有证据表明，炎性体成分的异常修饰导致了这种失调。这篇综述提供了对NLRP3炎性体通路内的PTM及其对信号级联的功能影响的见解。并强调了关于复杂的信号网络的悬而未决的问题。
