The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Caspase-11 auto-proteolysis is crucial for noncanonical inflammasome activation
Open accessAbstract
Intracellular LPS sensing by caspase-4/5/11 triggers proteolytic activation of pore-forming gasdermin D (GSDMD), leading to pyroptotic cell death in Gram-negative bacteria-infected cells. Involvement of caspase-4/5/11 and GSDMD in inflammatory responses, such as lethal sepsis, makes them highly desirable drug targets. Using knock-in (KI) mouse strains, we herein provide genetic evidence to show that caspase-11 auto-cleavage at the inter-subunit linker is essential for optimal catalytic activity and subsequent proteolytic cleavage of GSDMD. Macrophages from caspase-11–processing dead KI mice (Casp11Prc D285A/D285A) exhibit defective caspase-11 auto-processing and phenocopy Casp11−/− and caspase-11 enzymatically dead KI (Casp11Enz C254A/C254A) macrophages in attenuating responses to cytoplasmic LPS or Gram-negative bacteria infection. GsdmdD276A/D276A KI macrophages also fail to cleave GSDMD and are hypo-responsive to inflammasome stimuli, confirming that the GSDMD Asp276 residue is a nonredundant and indispensable site for proteolytic activation of GSDMD. Our data highlight the role of caspase-11 self-cleavage as a critical regulatory step for GSDMD processing and response against Gram-negative bacteria.
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Cites
Caspase-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
Self-citationInflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
Liu, X., Zhang, Z., Ruan, J., Pan, Y., Magupalli, V. G., Wu, H., & Lieberman, J. (2016) · Nature · doi:10.1038/nature18629 · Cited by 3,202
Cryopyrin activates the inflammasome in response to toxins and ATP
Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080
Pore-forming activity and structural autoinhibition of the gasdermin family
Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530
Self-citationInflammatory caspases are innate immune receptors for intracellular LPS
Shi, J., Zhao, Y., Wang, Y., Gao, W., Ding, J., Li, P., Hu, L., & Shao, F. (2014) · Nature · doi:10.1038/nature13683 · Cited by 2,285
Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
Broz, P., Ruby, T., Belhocine, K., Bouley, D. M., Kayagaki, N., Dixit, V. M., & Monack, D. M. (2012) · Nature · doi:10.1038/nature11419 · Cited by 535
Self-citationGuanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS
Pilla, D. M., Hagar, J. A., Haldar, A. K., Mason, A. K., Degrandi, D., Pfeffer, K., Ernst, R. K., Yamamoto, M., Miao, E. A., & Coers, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321700111 · Cited by 357
Non-canonical activation of inflammatory caspases by cytosolic LPS in innate immunity
Yang, J., Zhao, Y., & Shao, F. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.01.007 · Cited by 269
Cited by
The NLRP3 inflammasome: molecular activation and regulation to therapeutics
Swanson, K. V., Deng, M., & Ting, J. P.-Y. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0165-0 · Cited by 4,884
Blevins, H. M., Xu, Y., Biby, S., & Zhang, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.879021 · Cited by 587
A 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases
Barnett, K. C., Li, S., Liang, K., & Ting, J. P.-Y. (2023) · Cell · doi:10.1016/j.cell.2023.04.025 · Cited by 458
The Role of Microglia and the Nlrp3 Inflammasome in Alzheimer's Disease
Hanslik, K. L., & Ulland, T. K. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.570711 · Cited by 236
Intracellular Lipopolysaccharide Sensing as a Potential Therapeutic Target for Sepsis
Pfalzgraff, A., & Weindl, G. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.01.001 · Cited by 139
Metadata
- Authors
- Lee, B. L., Stowe, I. B., Gupta, A., Kornfeld, O. S., Roose-Girma, M., Anderson, K., Warming, S., Zhang, J., Lee, W. P., & Kayagaki, N.
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2018-08-22
- Volume
- 215
- Issue
- 9
- Pages
- 2279-2288
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- OpenAlex
- W2888308014
- Cited by
- 168
- References
- 9
- FWCI
- 4.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Lee, B. L., Stowe, I. B., Gupta, A., Kornfeld, O. S., Roose-Girma, M., Anderson, K., Warming, S., Zhang, J., Lee, W. P., & Kayagaki, N. (2018). Caspase-11 auto-proteolysis is crucial for noncanonical inflammasome activation. Journal of Experimental Medicine. https://doi.org/10.1084/jem.20180589
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