The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
MAVS Forms Functional Prion-like Aggregates to Activate and Propagate Antiviral Innate Immune Response
Open accessAbstract
SUMMARY In response to viral infection, RIG-I–like RNA helicases bind to viral RNA and activate the mitochondrial protein MAVS, which in turn activates the transcription factors IRF3 and NF-κB to induce type-I interferons. We have previously shown that RIG-I binds to unanchored lysine-63 (K63) polyubiquitin chains and that this binding is important for MAVS activation; however, the mechanism underlying MAVS activation is not understood. Here we show that viral infection induces the formation of very large MAVS aggregates, which potently activate IRF3 in the cytosol. We find that a fraction of recombinant MAVS protein forms fibrils capable of activating IRF3. Remarkably, the MAVS fibrils behave like prions and effectively convert endogenous MAVS into functional aggregates. We also show that, in the presence of K63 ubiquitin chains, RIG-I catalyzes the conversion of MAVS on the mitochondrial membrane to prion-like aggregates. These results suggest that a prion-like conformational switch of MAVS activates and propagates the antiviral signaling cascade.
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Cites
Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K. J., et al. (2006) · Nature · doi:10.1038/nature04734 · Cited by 3,888
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
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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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RIG-I-mediated antiviral responses to single-stranded RNA bearing 5’-phosphates
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Nucleic acid recognition by the innate immune system
Barbalat, R., Ewald, S. E., Mouchess, M. L., & Barton, G. M. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101340 · Cited by 577
RIGorous Detection: Exposing Virus Through RNA Sensing
Rehwinkel, J., & Reis e Sousa, C. (2010) · Science · doi:10.1126/science.1185068 · Cited by 163
The prion hypothesis: from biological anomaly to basic regulatory mechanism
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Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation
Liu, S., Cai, X., Wu, J., Cong, Q., Chen, X., Li, T., Du, F., Ren, J., Wu, Y.-T., Grishin, N. V., et al. (2015) · Science · doi:10.1126/science.aaa2630 · Cited by 1,927
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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
Roulois, D., Loo Yau, H., Singhania, R., Wang, Y., Danesh, A., Shen, S. Y., Han, H., Liang, G., Jones, P. A., Pugh, T. J., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.056 · Cited by 1,527
Metadata
- Authors
- Hou, F., Sun, L., Zheng, H., Skaug, B., Jiang, Q.-X., & Chen, Z. J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-08
- Volume
- 146
- Issue
- 3
- Pages
- 448-461
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2053476949
- Cited by
- 1,282
- References
- 7
- FWCI
- 30.80
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Hou, F., Sun, L., Zheng, H., Skaug, B., Jiang, Q.-X., & Chen, Z. J. (2011). MAVS Forms Functional Prion-like Aggregates to Activate and Propagate Antiviral Innate Immune Response. Cell. https://doi.org/10.1016/j.cell.2011.06.041
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