The NAIP/NLRC4 inflammasomes

被引:148
作者
Vance, Russell E. [1 ,2 ]
机构
[1] Howard Hughes Med Inst, Chevy Chase, MD 20815 USA
[2] Univ Calif Berkeley, Canc Res Lab, Berkeley, CA 94720 USA
基金
美国国家卫生研究院;
关键词
CAUSES AUTOINFLAMMATION; BACTERIAL LIGANDS; CRYSTAL-STRUCTURE; NLRC4; CAUSES; CELL-DEATH; RECOGNITION; ACTIVATION; PYROPTOSIS; FLAGELLIN; MUTATION;
D O I
10.1016/j.coi.2015.01.010
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Inflammasomes comprise a family of cytosolic multi-protein complexes that sense infection, or other threats, and initiate inflammation via the recruitment and activation of the Caspase-1 protease. Although the precise molecular mechanism by which most inflammasomes are activated remains a subject of considerable debate, the NAIP/NLRC4 subfamily of inflammasomes is increasingly well understood. A crystal structure of NLRC4 was recently reported, and a domain in NAIPs that recognizes bacterial ligands was identified. In addition, gain-of-function mutations in NLRC4 have been shown to cause an auto-inflammatory syndrome in humans. Lastly, the NAIP/NLRC4 inflammasome has been shown to provide a novel form of cell intrinsic defense against Salmonella infection, involving expulsion of infected cells from the intestinal epithelium.
引用
收藏
页码:84 / 89
页数:6
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