Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
Open accessAbstract
Inflammatory caspases (caspases 1, 4, 5 and 11) are activated in response to microbial infection and danger signals. When activated, they cleave mouse and human gasdermin D (GSDMD) after Asp276 and Asp275, respectively, to generate an N-terminal cleavage product (GSDMD-NT) that triggers inflammatory death (pyroptosis) and release of inflammatory cytokines such as interleukin-1β. Cleavage removes the C-terminal fragment (GSDMD-CT), which is thought to fold back on GSDMD-NT to inhibit its activation. However, how GSDMD-NT causes cell death is unknown. Here we show that GSDMD-NT oligomerizes in membranes to form pores that are visible by electron microscopy. GSDMD-NT binds to phosphatidylinositol phosphates and phosphatidylserine (restricted to the cell membrane inner leaflet) and cardiolipin (present in the inner and outer leaflets of bacterial membranes). Mutation of four evolutionarily conserved basic residues blocks GSDMD-NT oligomerization, membrane binding, pore formation and pyroptosis. Because of its lipid-binding preferences, GSDMD-NT kills from within the cell, but does not harm neighbouring mammalian cells when it is released during pyroptosis. GSDMD-NT also kills cell-free bacteria in vitro and may have a direct bactericidal effect within the cytosol of host cells, but the importance of direct bacterial killing in controlling in vivo infection remains to be determined.
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Membrane targeting enables GSDMD-N oligomerization, generating a pore responsible for rapid plasma membrane permeabilization.
“Membrane targeting enables GSDMD-N oligomerization, generating a pore that is responsible for rapid plasma membrane permeabilization [629–633].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [630]
Cleaved GSDMD-N translocates to the inner leaflet of the plasma membrane or bacterial plasma membrane, where it binds with high specificity to selected phosphoinositides or cardiolipin.
“Cleaved GSDMD-N acquires the ability to translocate to the inner leaflet of the plasma membrane (or the bacterial plasma membrane), where it binds with high specificity to selected phosphoinositides (or cardiolipin) [629, 630].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [630]
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- Authors
- Liu, X., Zhang, Z., Ruan, J., Pan, Y., Magupalli, V. G., Wu, H., & Lieberman, J.
- Affiliations
- Boston Children's Hospital (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Wu, Hao
- Lieberman, Judy
- Venue
- Nature
- Published
- 2016-07-06
- Volume
- 535
- Issue
- 7610
- Pages
- 153-158
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5539988
- OpenAlex
- W2462773201
- Cited by
- 3,202
- References
- 30
- Citations by year
- 2026: 323 · 2025: 356 · 2024: 407 · 2023: 478 · 2022: 497 · 2021: 369 · 2020: 298 · 2019: 201 · 2018: 138 · 2017: 105 · 2016: 26
- FWCI
- 81.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI123265, R01AI124491)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (DP1HD087988)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- gasdermin D, pyroptosis, inflammasome, caspase-11, pore formation, N-terminal domain, phosphoinositides, cardiolipin, phosphatidylserine, bacterial killing, innate immunity, programmed cell death, interleukin-1β release, GSDMA
- MeSH terms
- Pyroptosis, Gasdermins, Amino Acid Sequence, Animals, Cardiolipins, Cell Line, Cell Membrane, Cell Membrane Permeability, Escherichia coli, Humans, Liposomes, Listeria monocytogenes, Membrane Proteins, Mice, Inbred C57BL, Microscopy, Electron, Molecular Sequence Data, Mutation, Neoplasm Proteins, Phosphatidylserines, Staphylococcus aureus, Porosity, Conserved Sequence, Protein Structure, Tertiary, Phosphatidylinositol Phosphates, Protein Transport, Phosphate-Binding Proteins, Intracellular Signaling Peptides and Proteins, Microbial Viability, Mice, Protein Multimerization, Inflammasomes
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