炎症体
吡喃结构域
细胞生物学
信号转导衔接蛋白
促炎细胞因子
先天免疫系统
目标2
炎症
信号转导
上睑下垂
胞浆
化学
生物
免疫系统
免疫学
生物化学
酶
作者
Anil Akbal,Alesja Dernst,Marta Lovotti,Matthew Mangan,Róisín M. McManus,Eicke Latz
标识
DOI:10.1038/s41423-022-00922-w
摘要
NOD-, LRR-, and pyrin domain-containing 3 (NLRP3) is a cytosolic innate immune sensor of cellular stress signals, triggered by infection and sterile inflammation. Upon detection of an activating stimulus, NLRP3 transitions from an inactive homo-oligomeric multimer into an active multimeric inflammasome, which promotes the helical oligomeric assembly of the adaptor molecule ASC. ASC oligomers provide a platform for caspase-1 activation, leading to the proteolytic cleavage and activation of proinflammatory cytokines in the IL-1 family and gasdermin D, which can induce a lytic form of cell death. Recent studies investigating both the cellular requirement for NLRP3 activation and the structure of NLRP3 have revealed the complex regulation of NLRP3 and the multiple steps involved in its activation. This review presents a perspective on the biochemical and cellular processes controlling the assembly of the NLRP3 inflammasome with particular emphasis on structural regulation and the role of organelles. We also highlight the latest research on metabolic control of this inflammatory pathway and discuss promising clinical targets for intervention.
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