‘Hints’ in the killer protein gasdermin D: unveiling the secrets of gasdermins driving cell death
Open accessAbstract
Pyroptosis is a lytic form of cell death distinguished from apoptosis, ferroptosis, necrosis, necroptosis, NETosis, oncosis, pyronecrosis and autophagy. Proinflammatory caspases cleave a gasdermin D (GSDMD) protein to generate a 31 kDa N-terminal domain. The cleavage relieves the intramolecular inhibition on the gasdermin-N domain, which then moves to the plasma membrane to exhibit pore-forming activity. Thus, GSDMD acts as the final and direct executor of pyroptotic cell death. Owing to the selective targeting of the inner leaflet of the plasma membrane with the pore-forming that determines pyroptotic cell death, GSDMD could be a potential target to control cell death or extracellular bacterial infections. Intriguingly, other gasdermin family members also share similar N-terminal domains, but they present different cell death programs. Herein, we summarize features and functions of the novel player proteins in cell death, including GSDMD triggering pyroptosis, Gsdma3/GSDMA initiating autophagy/apoptosis and DFNA5 inducing apoptosis/secondary necrosis. The gasdermin N terminus appears to be a novel pore-forming protein. This provides novel insight into the underlying roles and mechanisms of lytic or nonlytic forms of programmed cell death, as well as their potential applications in inflammation-associated diseases.
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Once activated beyond a specific threshold, inflammatory caspases precipitate pyroptosis by catalyzing proteolytic cleavage of GSDMD.
“Once activated beyond a specific threshold, inflammatory caspases precipitate pyroptosis by catalyzing the proteolytic cleavage of GSDMD [621, 626, 627].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [627]
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- Authors
- Qiu, S., Liu, J., & Xing, F.
- Affiliations
- Jinan University (CN)
- Corresponding author
- Liu, Jing
- Xing, Feiyue
- ORCID
- Xing, Feiyue
- Venue
- Cell Death & Differentiation
- Published
- 2017-03-03
- Volume
- 24
- Issue
- 4
- Pages
- 588-596
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- PMC
- PMC5384029
- OpenAlex
- W2600940366
- Cited by
- 111
- References
- 58
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 12 · 2023: 20 · 2022: 22 · 2021: 19 · 2020: 11 · 2019: 8 · 2018: 6 · 2017: 3
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell Death and Differentiation (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (30971465, 81172824)
- 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, pore-forming proteins, programmed cell death, gasdermin E, autophagy, apoptosis, secondary necrosis, caspase cleavage, plasma membrane targeting, inflammation, bacterial infection
- MeSH terms
- Pyroptosis, Gasdermins, Autophagy, Humans, Neoplasm Proteins, Receptors, Estrogen, Saccharomyces cerevisiae, Signal Transduction, Transforming Growth Factor beta, Caspases, Phosphate-Binding Proteins, Saccharomyces cerevisiae Proteins, Intracellular Signaling Peptides and Proteins
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