信号转导衔接蛋白
内部收益率3
特里夫
细胞生物学
先天免疫系统
生物
刺
坦克结合激酶1
丝氨酸
信号转导
Toll样受体
磷酸化
受体
蛋白激酶A
MAP激酶激酶激酶
生物化学
工程类
航空航天工程
作者
Siqi Liu,Xin Cai,Jiaxi Wu,Qian Cong,Xiang Chen,Tuo Li,Fenghe Du,Junyao Ren,Ya Fei Wu,Nick V. Grishin,Zhijian J. Chen
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2015-03-13
卷期号:347 (6227)
被引量:1322
标识
DOI:10.1126/science.aaa2630
摘要
During virus infection, the adaptor proteins MAVS and STING transduce signals from the cytosolic nucleic acid sensors RIG-I and cGAS, respectively, to induce type I interferons (IFNs) and other antiviral molecules. Here we show that MAVS and STING harbor two conserved serine and threonine clusters that are phosphorylated by the kinases IKK and/or TBK1 in response to stimulation. Phosphorylated MAVS and STING then bind to a positively charged surface of interferon regulatory factor 3 (IRF3) and thereby recruit IRF3 for its phosphorylation and activation by TBK1. We further show that TRIF, an adaptor protein in Toll-like receptor signaling, activates IRF3 through a similar phosphorylation-dependent mechanism. These results reveal that phosphorylation of innate adaptor proteins is an essential and conserved mechanism that selectively recruits IRF3 to activate the type I IFN pathway.
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