The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
The Gasdermin‐D pore acts as a conduit for IL‐1β secretion in mice
Open accessAbstract
The pro‐inflammatory cytokine IL‐1β is well known for its role in host defense and the initiation of potent inflammatory responses. It is processed from its inactive pro‐form by the inflammatory caspase‐1 into its mature bioactive form, which is then released from the cell via an unconventional secretion mechanism. Recently, gasdermin‐D has been identified as a new target of caspase‐1. After proteolytical cleavage of gasdermin‐D, the N‐terminal fragment induces pyroptosis, a lytic cell death, by forming large permeability pores in the plasma membrane. Here we show using the murine system that gasdermin‐D is required for IL‐1β secretion by macrophages, dendritic cells and partially in neutrophils, and that secretion is a cell‐lysis‐independent event. Liposome transport assays in vitro further demonstrate that gasdermin‐D pores are large enough to allow the direct release of IL‐1β. Moreover, IL‐18 and other small soluble cytosolic proteins can also be released in a lysis‐independent but gasdermin‐D‐dependent mode, suggesting that the gasdermin‐D pores allow passive the release of cytosolic proteins in a size‐dependent manner.
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Cites
Antiinflammatory Therapy with Canakinumab for Atherosclerotic Disease
Ridker, P. M., Everett, B. M., Thuren, T., MacFadyen, J. G., Chang, W. H., Ballantyne, C., Fonseca, F., Nicolau, J., Koenig, W., Anker, S. D., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1707914 · Cited by 9,482
Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
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Gout-associated uric acid crystals activate the NALP3 inflammasome
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,873
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
Inflammasomes: mechanism of assembly, regulation and signalling
Broz, P., & Dixit, V. M. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.58 · Cited by 3,500
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
Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin
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Pore-forming activity and structural autoinhibition of the gasdermin family
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A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,572
Cited by
The gasdermins, a protein family executing cell death and inflammation
Broz, P., Pelegrín, P., & Shao, F. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-019-0228-2 · Cited by 1,641
Pyroptosis versus necroptosis: similarities, differences, and crosstalk
Frank, D., & Vince, J. E. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0212-6 · Cited by 1,062
Autophagy-Independent Functions of the Autophagy Machinery
Galluzzi, L., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.026 · Cited by 863
“However, this model cannot be easily reconciled with the fact that gasdermin D (GSDMD), a core component of the molecular mechanism for pyroptosis (Box 2), is also required for IL-1b secretion by macrophages (Heilig et al., 2018).”
ResultGenomic and drug target evaluation of 90 cardiovascular proteins in 30,931 individuals
Folkersen, L., Gustafsson, S., Wang, Q., Hansen, D. H., Hedman, Å. K., Schork, A., Page, K., Zhernakova, D. V., Wu, Y., Peters, J., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00287-2 · Cited by 705
Noncanonical inflammasome signaling elicits gasdermin D–dependent neutrophil extracellular traps
Chen, K. W., Monteleone, M., Boucher, D., Sollberger, G., Ramnath, D., Condon, N. D., von Pein, J. B., Broz, P., Sweet, M. J., & Schroder, K. (2018) · Science Immunology · doi:10.1126/sciimmunol.aar6676 · Cited by 639
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Metadata
- Authors
- Heilig, R., Dick, M. S., Sborgi, L., Meunier, E., Hiller, S., & Broz, P.
- Venue
- European Journal of Immunology
- Publisher
- Wiley
- Published
- 2018-01-15
- Volume
- 48
- Issue
- 4
- Pages
- 584-592
- ISSN
- 0014-2980 (ISSN-L)
- 1521-4141
- OpenAlex
- W2779886179
- Cited by
- 377
- References
- 53
- FWCI
- 8.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Heilig, R., Dick, M. S., Sborgi, L., Meunier, E., Hiller, S., & Broz, P. (2018). The Gasdermin‐D pore acts as a conduit for IL‐1β secretion in mice. European Journal of Immunology. https://doi.org/10.1002/eji.201747404
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