期刊
NATURE IMMUNOLOGY
卷 15, 期 12, 页码 1126-1133出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ni.3015
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资金
- National Basic Research Program of China [2014CB910800]
- National Natural Science Foundation of China [81330078, 81222040]
- Doctoral Fund of the Ministry of Education of China [20123402120001, 20123402110010]
- One Hundred Person Project
- Fundamental Research Funds for the Central Universities
The NLRP3 inflammasome functions as a crucial component of the innate immune system in recognizing viral infection, but the mechanism by which viruses activate this inflammasome remains unclear. Here we found that inhibition of the serine-threonine kinases RIP1 (RIPK1) or RIP3 (RIPK3) suppressed RNA virus-induced activation of the NLRP3 inflammasome. Infection with an RNA virus initiated assembly of the RIP1-RIP3 complex, which promoted activation of the GTPase DRP1 and its translocation to mitochondria to drive mitochondrial damage and activation of the NLRP3 inflammasome. Notably, the RIP1-RIP3 complex drove the NLRP3 inflammasome independently of MLKL, an essential downstream effector of RIP1-RIP3-dependent necrosis. Together our results reveal a specific role for the RIP1-RIP3-DRP1 pathway in RNA virus-induced activation of the NLRP3 inflammasome and establish a direct link between inflammation and cell-death signaling pathways.
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