The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity
Open accessAbstract
Host-protective caspase-1 activity must be tightly regulated to prevent pathology, but mechanisms controlling the duration of cellular caspase-1 activity are unknown. Caspase-1 is activated on inflammasomes, signaling platforms that facilitate caspase-1 dimerization and autoprocessing. Previous studies with recombinant protein identified a caspase-1 tetramer composed of two p20 and two p10 subunits (p20/p10) as an active species. In this study, we report that in the cell, the dominant species of active caspase-1 dimers elicited by inflammasomes are in fact full-length p46 and a transient species, p33/p10. Further p33/p10 autoprocessing occurs with kinetics specified by inflammasome size and cell type, and this releases p20/p10 from the inflammasome, whereupon the tetramer becomes unstable in cells and protease activity is terminated. The inflammasome–caspase-1 complex thus functions as a holoenzyme that directs the location of caspase-1 activity but also incorporates an intrinsic self-limiting mechanism that ensures timely caspase-1 deactivation. This intrinsic mechanism of inflammasome signal shutdown offers a molecular basis for the transient nature, and coordinated timing, of inflammasome-dependent inflammatory responses.
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Cites
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Self-citationCaspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686
Cryopyrin activates the inflammasome in response to toxins and ATP
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A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
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Altered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme
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Self-citation
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MCC950 directly targets the NLRP3 ATP-hydrolysis motif for inflammasome inhibition
Coll, R. C., Hill, J. R., Day, C. J., Zamoshnikova, A., Boucher, D., Massey, N. L., Chitty, J. L., Fraser, J. A., Jennings, M. P., Robertson, A. A. B., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0277-7 · Cited by 1,014
Self-citationThe lncRNA Neat1 promotes activation of inflammasomes in macrophages
Zhang, P., Cao, L., Zhou, R., Yang, X., & Wu, M. (2019) · Nature Communications · doi:10.1038/s41467-019-09482-6 · Cited by 499
Inflammasome Activation Triggers Blood Clotting and Host Death through Pyroptosis
Wu, C., Lu, W., Zhang, Y., Zhang, G., Shi, X., Hisada, Y., Grover, S. P., Zhang, X., Li, L., Xiang, B., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.04.003 · Cited by 417
Metadata
- Authors
- Boucher, D., Monteleone, M., Coll, R. C., Chen, K. W., Ross, C. M., Teo, J. L., Gomez, G. A., Holley, C. L., Bierschenk, D., Stacey, K. J., Yap, A. S., Bezbradica, J. S., & Schroder, K.
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2018-02-06
- Volume
- 215
- Issue
- 3
- Pages
- 827-840
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2791444686
- Cited by
- 560
- References
- 22
- FWCI
- 14.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Boucher, D., Monteleone, M., Coll, R. C., Chen, K. W., Ross, C. M., Teo, J. L., Gomez, G. A., Holley, C. L., Bierschenk, D., Stacey, K. J., Yap, A. S., Bezbradica, J. S., & Schroder, K. (2018). Caspase-1 self-cleavage is an intrinsic mechanism to terminate inflammasome activity. Journal of Experimental Medicine. https://doi.org/10.1084/jem.20172222
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