The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Riplet/RNF135, a RING Finger Protein, Ubiquitinates RIG-I to Promote Interferon-β Induction during the Early Phase of Viral Infection
Open accessAbstract
RIG-I (retinoic acid-inducible gene-I), a cytoplasmic RNA helicase, interacts with IPS-1/MAVS/Cardif/VISA, a protein on the outer membrane of mitochondria, to signal the presence of virus-derived RNA and induce type I interferon production. Activation of RIG-I requires the ubiquitin ligase, TRIM25, which mediates lysine 63-linked polyubiquitination of the RIG-I N-terminal CARD-like region. However, how this modification proceeds for activation of IPS-1 by RIG-I remains unclear. Here we identify an alternative factor, Riplet/RNF135, that promotes RIG-I activation independent of TRIM25. The Riplet/RNF135 protein consists of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs, and shows sequence similarity to TRIM25. Immunoprecipitation analyses demonstrated that the C-terminal helicase and repressor domains of RIG-I interact with the Riplet/RNF135 C-terminal region, whereas the CARD-like region of RIG-I is dispensable for this interaction. Riplet/RNF135 promotes lysine 63-linked polyubiquitination of the C-terminal region of RIG-I, modification of which differs from the N-terminal ubiquitination by TRIM25. Overexpression and knockdown analyses revealed that Riplet/RNF135 promotes RIG-I-mediated interferon-beta promoter activation and inhibits propagation of the negative-strand RNA virus, vesicular stomatitis virus. Our data suggest that Riplet/RNF135 is a novel factor of the RIG-I pathway that is involved in the evoking of human innate immunity against RNA virus infection, and activates RIG-I through ubiquitination of its C-terminal region. We infer that a variety of RIG-I-ubiquitinating molecular complexes sustain RIG-I activation to modulate RNA virus replication in the cytoplasm.
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IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
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5'-Triphosphate RNA Is the Ligand for RIG-I
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Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
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TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
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Cited by
Immune Signaling by RIG-I-like Receptors
Loo, Y.-M., & Gale, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.05.003 · Cited by 1,875
Innate Immune Pattern Recognition: A Cell Biological Perspective
Brubaker, S. W., Bonham, K. S., Zanoni, I., & Kagan, J. C. (2015) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112240 · Cited by 1,475
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
Lee (2019) · doi:10.1038/s12276-019-0299-y · Cited by 635
Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5
Brisse, M., & Ly, H. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01586 · Cited by 365
Metadata
- Authors
- Oshiumi, H., Matsumoto, M., Hatakeyama, S., & Seya, T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 284
- Issue
- 2
- Pages
- 807-817
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2066691052
- Cited by
- 353
- References
- 34
- FWCI
- 6.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Oshiumi, H., Matsumoto, M., Hatakeyama, S., & Seya, T. (2009). Riplet/RNF135, a RING Finger Protein, Ubiquitinates RIG-I to Promote Interferon-β Induction during the Early Phase of Viral Infection. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m804259200
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