Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2

By Takeshi Saito, R. Hirai, Y. Loo, D. Owen, C. L. Johnson, Sangita C. Sinha, Shizuo Akira, T. Fujita, M. Gale. Proceedings of the National Academy of Sciences of the United States of America, 2007

783 citations recorded by the source corpus.

Subfields: Epidemiology, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/faa92c99ab49ece3f6587fd344f7d24bf07c2910

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Citations in the corpus

MDA5/RIG-I and virus recognition. (2008, methodology): “A C-terminal portion of RIG-I, designated the repressor domain (RD), was shown to inhibit the triggering of RIG-I signaling in the steady state [8].”
Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures. (2008, background): “A third member of the helicase family (LGP2) has also been described; this protein lacks the CARD domains present in mda-5 and RIG-I and appears to function as a negative regulator of IFN production (Rothenfusser et al., 2005; Yoneyama et al., 2005; Saito et al., 2007).”
Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5 (2015, positive): “On the contrary, the pincer domain is required to maintain the auto-repressed state since upon its deletion, CARD-hel become constitutively active, a finding that was initially misinterpreted as indicative of CTD bearing a repressor activity when testing the truncated RIG-I 1–734 (denoted Δ[β13-pinc”
RNA recognition and signal transduction by RIG‐I‐like receptors (2009, background): “Alternatively, the C-terminal portion of LGP2, which can function as RD, may directly inhibit the self-dimerization of activated RIG-I (37).”
Structural Basis of RNA Recognition and Activation by Innate Immune Receptor RIG-I (2011, background): “It has been proposed that RIG-I exists in an auto-inhibited stat”
Structural insights into RNA recognition by RIG-I (2011, positive): “The function of LGP-2 is less clearly defined, as it can act positively or negatively upon activation by different viruses (Saito et al., 2007; Satoh et al., 2010).”
DUSP11-mediated control of 5′-triphosphate RNA regulates RIG-I sensitivity (2020, methodology): “We used the 5′ untranslated region (UTR) of the HCV RNA, as its expression is immunostimulatory (Saito et al. 2007).”
A structure-based model of RIG-I activation. (2012, background): “Despite initial indications that dimerization or oligomerization of RIG-I would be essential for its activation (Saito et al. 2007) and that unlikely cartoons for the RIG-I dimer have been proposed (Cui et al. 2008; Hou et al. 2011), there is no indication from structural and biophysical studies…”
Innate Immunity to Virus Infection (2009, background): “The helicase domain and RD are important for the recognition of these RNAs, while the CARDs are essential for triggering intracellular signaling cascades (6, 12).”