期刊
EBIOMEDICINE
卷 9, 期 -, 页码 195-206出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ebiom.2016.06.015
关键词
RIG-I; HDAC6; Deacetylation; HCV; West Nile virus; Interferon; Innate immunity
资金
- NIH [AI118916, AI083019, AI098943, AI100625, AI104002]
- MOST [102-2320-B-002-044-MY2]
- NHRI [NHRI-EX104- 10417SC]
Retinoic acid inducible gene-I (RIG-I) is a cytosolic pathogen recognition receptor that initiates the immune response against many RNA viruses. Upon RNA ligand binding, RIG-I undergoes a conformational change facilitating its homo-oligomerization and activation that results in its translocation from the cytosol to intracellular membranes to bind its signaling adaptor protein, mitochondrial antiviral-signaling protein (MAVS). Here we show that RIG-I activation is regulated by reversible acetylation. Acetyl-mimetic mutants of RIG-I do not form virus-induced homo-oligomers, revealing that acetyl-lysine residues of the RIG-I repressor domain prevent assembly to active homo-oligomers. During acute infection, deacetylation of RIG-I promotes its oligomerization upon ligand binding. We identify histone deacetylase 6 (HDAC6) as the deacetylase that promotes RIG-I activation and innate antiviral immunity to recognize and restrict RNA virus infection. (C) 2016 The Authors. Published by Elsevier B.V.
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