The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
Open accessAbstract
RIG-I is a cytosolic pathogen recognition receptor that engages viral RNA in infected cells to trigger innate immune defenses through its adaptor protein MAVS. MAVS resides on mitochondria and peroxisomes, but how its signaling is coordinated among these organelles has not been defined. Here we show that a major site of MAVS signaling is the mitochondrial-associated membrane (MAM), a distinct membrane compartment that links the endoplasmic reticulum to mitochondria. During RNA virus infection, RIG-I is recruited to the MAM to bind MAVS. Dynamic MAM tethering to mitochondria and peroxisomes then coordinates MAVS localization to form a signaling synapse between membranes. Importantly, the hepatitis C virus NS3/4A protease, which cleaves MAVS to support persistent infection, targets this synapse for MAVS proteolysis from the MAM, but not from mitochondria, to ablate RIG-I signaling of immune defenses. Thus, the MAM mediates an intracellular immune synapse that directs antiviral innate immunity.
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Citations
Cites
A role for mitochondria in nlrp3 inflammasome activation
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STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
Ishikawa, H., Ma, Z., & Barber, G. N. (2009) · Nature · doi:10.1038/nature08476 · Cited by 2,759 · cited 1×
“STING, a putative RIG-I signaling cofactor and IPS-1 binding protein, also may have MAM localization, but this localization is likely specific to cell type and context (30).”
BackgroundMitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
Meylan, E., Curran, J., Hofmann, K., Moradpour, D., Binder, M., Bartenschlager, R., & Tschopp, J. (2005) · Nature · doi:10.1038/nature04193 · Cited by 2,401
Distinct RIG-I and MDA5 Signaling by RNA Viruses in Innate Immunity
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Self-citationMitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway
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Mitofusin 2 Inhibits Mitochondrial Antiviral Signaling
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Cited by
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
Mitochondria in the Regulation of Innate and Adaptive Immunity
Weinberg, S. E., Sena, L. A., & Chandel, N. S. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.002 · Cited by 960
Mitochondria: master regulators of danger signalling
Galluzzi, L., Kepp, O., & Kroemer, G. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3479 · Cited by 733
The Adaptor MAVS Promotes NLRP3 Mitochondrial Localization and Inflammasome Activation
Subramanian, N., Natarajan, K., Clatworthy, M. R., Wang, Z., & Germain, R. N. (2013) · Cell · doi:10.1016/j.cell.2013.02.054 · Cited by 678
Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions
Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625
Metadata
- Authors
- Horner, S. M., Liu, H. M., Park, H. S., Briley, J., & Gale, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-08-15
- Volume
- 108
- Issue
- 35
- Pages
- 14590-14595
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1998332163
- Cited by
- 491
- References
- 8
- FWCI
- 12.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Horner, S. M., Liu, H. M., Park, H. S., Briley, J., & Gale, M. (2011). Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1110133108
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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