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Structural and biochemical studies of RIG-I antiviral signaling

Protein & Cell 2013年第2期4卷 142-154页

作者： Miao Feng Zhanyu Ding Liang Xu Liangliang Kong Wenjia Wang Shi Jiao Zhubing Shi Mark IGreene Yao Cong Zhaocai Zhou State Key Laboratory of Cell Biology Institute of Biochemistry and Cell BiologyShanghai Institutes for Biological SciencesChinese Academy of SciencesShanghai 200031China State Key Laboratory of Molecular Biology Institute of Biochemistry and Cell BiologyShanghai Institutes for Biological SciencesChinese Academy of SciencesShanghai 200031China Department of Pathology and Laboratory Medicine University of PennsylvaniaPA 19104USA

Retinoic acid-inducible gene I(RIG-I)is an important pattern recognition receptor that detects viral RNA and triggers the production of type-I interferons through the downstream adaptor MAVS(also called IPS-1,CARDIF,or VISA).A series of structural studies have elaborated some of the mechanisms of dsRNA recognition and activation of *** studies have proposed that K63-linked ubiquitination of,or unanchored K63-linked polyubiquitin binding to RIG-I positively regulates MAVS-mediated antiviral *** phos-phorylation of RIG-I appears to play an inhibitory role in controlling RIG-I antiviral signal *** we performed a combined structural and biochemical study to further define the regulatory features of RIG-I *** and dsRNA binding triggered dimeriza-tion of RIG-I with conformational rearrangements of the tandem CARD *** length RIG-I appeared to form a complex with dsRNA in a 2:2 molar ***-pared with the previously reported crystal structures of RIG-I in inactive state,our electron microscopic struc-ture of full length RIG-I in complex with blunt-ended dsRNA,for the first time,revealed an exposed active conformation of the CARD ***,we found that purified recombinant RIG-I proteins could bind to the CARD domain of MAVS independently of dsRNA,while S8E and T170E phosphorylation-mimick-ing mutants of RIG-I were defective in binding E3 ligase TRIM25,unanchored K63-linked polyubiquitin,and MAVS regardless of *** findings suggested that phosphorylation of RIG inhibited downstream signaling by impairing RIG-I binding with polyubiquitin and its interaction with MAVS.

关键词： RIG-I MAVS antiviral signaling polyubiq-uitin phosphorylation

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