ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon

Jenish R. Patel, Ankur Jain, Yi Ying Chou, Alina Baum, Taekjip Ha, Adolfo García-Sastre

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100 Scopus citations


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.

Original languageEnglish
Pages (from-to)780-787
Number of pages8
JournalEMBO Reports
Issue number9
StatePublished - Sep 2013


  • ATP
  • Defective interfering RNA
  • Interferon
  • Oligomerization
  • RIG-I


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