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RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
Open accessAbstract
RIPK3 and its substrate MLKL are essential for necroptosis, a lytic cell death proposed to cause inflammation via the release of intracellular molecules. Whether and how RIPK3 might drive inflammation in a manner independent of MLKL and cell lysis remains unclear. Here we show that following LPS treatment, or LPS-induced necroptosis, the TLR adaptor protein TRIF and inhibitor of apoptosis proteins (IAPs: X-linked IAP, cellular IAP1 and IAP2) regulate RIPK3 and MLKL ubiquitylation. Hence, when IAPs are absent, LPS triggers RIPK3 to activate caspase-8, promoting apoptosis and NLRP3–caspase-1 activation, independent of RIPK3 kinase activity and MLKL. In contrast, in the absence of both IAPs and caspase-8, RIPK3 kinase activity and MLKL are essential for TLR-induced NLRP3 activation. Consistent with in vitro experiments, interleukin-1 (IL-1)-dependent autoantibody-mediated arthritis is exacerbated in mice lacking IAPs, and is reduced by deletion of RIPK3, but not MLKL. Therefore RIPK3 can promote NLRP3 inflammasome and IL-1β inflammatory responses independent of MLKL and necroptotic cell death.
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Metadata
- Authors
- Lawlor, K. E., Khan, N., Mildenhall, A., Gerlic, M., Croker, B. A., D’Cruz, A. A., Hall, C., Kaur Spall, S., Anderton, H., Masters, S. L., Rashidi, M., Wicks, I. P., Alexander, W. S., Mitsuuchi, Y., Benetatos, C. A., Condon, S. M., Wong, W. W.-L., Silke, J., Vaux, D. L., & Vince, J. E.
- Venue
- Nature Communications
- Published
- 2015-02-18
- Volume
- 6
- Issue
- 1
- Pages
- 6282-6282
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2008961838
- Cited by
- 649
- References
- 66
- FWCI
- 21.87
- Type
- journal article
- Language
- en
- Open access
- gold
- Licence
- creativecommons.org/licenses/by/4.0 (tdm)
- creativecommons.org/licenses/by/4.0 (vor)
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