Journal
NATURE IMMUNOLOGY
Volume 12, Issue 1, Pages 37-U56Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ni.1963
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- IRYO HOJIN SHADAN JIKOKAI
- Astellas Foundation for Research on Metabolic Disorders
- Kanae Foundation for the Promotion of Medical Science
- Kato Memorial Bioscience Foundation
- Yasuda Medical Foundation
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The poly(ADP-ribose) polymerases (PARPs) participate in many biological and pathological processes. Here we report that the PARP-13 shorter isoform (ZAPS), rather than the full-length protein (ZAP), was selectively induced by 5'-triphosphate-modified RNA (3pRNA) and functioned as a potent stimulator of interferon responses in human cells mediated by the RNA helicase RIG-I. ZAPS associated with RIG-I to promote the oligomerization and ATPase activity of RIG-I, which led to robust activation of IRF3 and NF-kappa B transcription factors. Disruption of the gene encoding ZAPS resulted in impaired induction of interferon-alpha (IFN-alpha), IFN-beta and other cytokines after viral infection. These results indicate that ZAPS is a key regulator of RIG-I signaling during the innate antiviral immune response, which suggests its possible use as a therapeutic target for viral control.
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