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您的检索式：作者名="Mark IGreene"
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| 1 | Structural and biochemical studies of RIG-I antiviral signaling显示文摘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 RIG-I.Recent studies have proposed that K63-linked ubiquitination of,or unanchored K63-linked polyubiquitin binding to RIG-I positively regulates MAVS-mediated antiviral signaling.Conversely phos-phorylation of RIG-I appears to play an inhibitory role in controlling RIG-I antiviral signal transduction.Here we performed a combined structural and biochemical study to further define the regulatory features of RIG-I signaling.ATP and dsRNA binding triggered dimeriza-tion of RIG-I with conformational rearrangements of the tandem CARD domains.Full length RIG-I appeared to form a complex with dsRNA in a 2:2 molar ratio.Com-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 domains.Moreover,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 dsRNA.These findings suggested that phosphorylation of RIG inhibited downstream signaling by impairing RIG-I binding with polyubiquitin and its interaction with MAVS. | Miao Feng Zhanyu Ding Liang Xu Liangliang Kong Wenjia Wang Shi Jiao Zhubing Shi Mark IGreene Yao Cong Zhaocai Zhou | 2013 | Protein & Cell2013，4，2： | 2 |
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