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Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization.
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- المؤلفون: Liman Zhang1,2; Shuobing Chen3,4; Jianbin Ruan1,2; Jiayi Wu3,4; Tong, Alexander B.1,2; Qian Yin1,2; Yang Li1,2; David, Liron1,2; Lu, Alvin1,2; Wei Li Wang4,5; Marks, Carolyn6; Qi Ouyang3; Xinzheng Zhang7; Youdong Mao3,4,5 ; Hao Wu1,2
- المصدر:
Science. 10/23/2015, Vol. 350 Issue 1659, p404-409. 6p.
- الموضوع:
- معلومة اضافية
- نبذة مختصرة :
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. [ABSTRACT FROM AUTHOR]
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