title: ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon.
abstract: The cytosolic pathogen sensor RIG-I is activated by RNAs with exposed 5'-triphosphate (5'-ppp) and terminal double-stranded structures, such as those that are generated during viral infection. RIG-I has been shown to translocate on dsRNA in an ATP-dependent manner. However, the precise role of the ATPase activity in RIG-I activation remains unclear. Using in vitro-transcribed Sendai virus defective interfering RNA as a model ligand, we show that RIG-I oligomerizes on 5'-ppp dsRNA in an ATP hydrolysis-dependent and dsRNA length-dependent manner, which correlates with the strength of type-I interferon (IFN-I) activation. These results establish a clear role for the ligand-induced ATPase activity of RIG-I in the stimulation of the IFN response.
authors.affiliation: 1] Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA [2] Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.
authors.forename: Jenish R
authors.initials: JR
authors.lastname: Patel
authors.forename: Ankur
authors.initials: A
authors.lastname: Jain
authors.forename: Yi-ying
authors.initials: YY
authors.lastname: Chou
authors.forename: Alina
authors.initials: A
authors.lastname: Baum
authors.forename: Taekjip
authors.initials: T
authors.lastname: Ha
authors.forename: Adolfo
authors.initials: A
authors.lastname: García-Sastre
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D057809:HEK293 Cells; D006801:Humans; D006868:Hydrolysis; D007370:Interferon Type I / Q000378:metabolism*; D011485:Protein Binding; D055503:Protein Multimerization; D020365:RNA Helicases / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D029082:Sendai virus
chemical_list: D007370:Interferon Type I; D012367:RNA, Viral; D000255:Adenosine Triphosphate; D020365:RNA Helicases