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论文成果
Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization
发布时间：2020-03-10点击次数：
影响因子：
47.0
DOI码：
10.1126/science.aac5789
发表刊物：
Science
刊物所在地：
USA
摘要：
The NLR family apoptosis inhibitory proteins (NAIPs) bind conserved bacterial ligands, such as the bacterial rod protein PrgJ, and recruit NLR family CARD-containing protein 4 (NLRC4) as the inflammasome adapter to activate innate immunity. We found that the PrgJ-NAIP2-NLRC4 inflammasome is assembled into multisubunit disk-like structures through a unidirectional adenosine triphosphatase polymerization, primed with a single PrgJ-activated NAIP2 per disk. Cryo-electron microscopy (cryo-EM) reconstruction at subnanometer resolution revealed a ~90° hinge rotation accompanying NLRC4 activation. Unlike in the related heptameric Apaf-1 apoptosome, in which each subunit needs to be conformationally activated by its ligand before assembly, a single PrgJ-activated NAIP2 initiates NLRC4 polymerization in a domino-like reaction to promote the disk assembly. These insights reveal the mechanism of signal amplification in NAIP-NLRC4 inflammasomes.
论文类型：
期刊论文
学科门类：
理学
文献类型：
J
卷号：
350
页面范围：
404-409
是否译文：
否
发表时间：
2015-10-23
收录刊物：
SCI
附件：