NDLI: Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization

Content Provider	PubMed Central
Author	Zhang, Liman Chen, Shuobing Ruan, Jianbin Wu, Jiayi Tong, Alexander B. Yin, Qian Li, Yang David, Liron Lu, Alvin Wang, Wei Li Marks, Carolyn Ouyang, Qi Zhang, Xinzheng Mao, Youdong Wu, Hao
Abstract	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.
Related Links	http://dx.doi.org/10.1126/science.aac5789
Ending Page	409
Page Count	6
Starting Page	404
File Format	PDF
ISSN	00368075
e-ISSN	10959203
Journal	Science (New York, N.Y.)
Issue Number	6259
Volume Number	350
Language	English
Publisher Date	2015-10-23
Access Restriction	Open
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	History and Philosophy of Science

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