ArticleThe EMBO journal2024
Gasdermin D cysteine residues synergistically control its palmitoylation-mediated membrane targeting and assembly.
Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- The role of protein palmitoylation in disease pathogenesis and therapeutic innovation.Annals of medicine · 2026Review
- Igniting antitumour immunity with cancer cell pyroptosis.Nature reviews. Cancer · 2026Review
- Structural basis of GSDME pore formation and its regulation by S-palmitoylation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism and plasticity of primitive pyroptosis.Science advances · 2026Article
- Theme and variations: activation and regulation of gasdermin-mediated inflammation.Biochemical Society transactions · 2026Review
- Bottom-up reconstitution of model membrane systems: a mini-review.Biochemical Society transactions · 2026Review
- Direct visualization of native GSDMD pores reveals lipid-driven stabilization during pyroptosis.Science advances · 2026Article
- Palmitoylation-dependent regulation of innate and adaptive immunity: molecular insights and translational opportunities.Cellular & molecular biology letters · 2026Review
- Pyroptosis: Turning Up the Heat on Cancer.Annual review of immunology · 2026Review
- Structural basis and regulation of GSDME pore formation.Nature communications · 2026Article
- Gasdermins against intracellular bacterial pathogens.Nature microbiology · 2026Review
- Microtubule detyrosination links inflammasome activation to apoptotic cell death in macrophages upon influenza A virus infection.Journal of virology · 2026Article
- Teleost GSDMEc regulates GSDMEa-mediated pyroptosis.Journal of advanced research · 2026Article
- Protein S-Palmitoylation as Potential Therapeutic Target for Dermatoses.Biomolecules · 2025Review
- Loss of ADAM15 prevents necroptosis induction by partial RIPK1 degradation due to enhanced TNF-R1 surface expression and basal caspase-8 activation.Cell communication and signaling : CCS · 2025Article
- Disulfiram inhibits Gasdermin D pores formation and improves insulin-dependent glucose uptake and glucose homeostasis in skeletal muscle of obesity-induced insulin-resistant mice.Scientific reports · 2025Article
- Gasdermins: multifunctional effectors of membrane permeabilization across cellular compartments.The FEBS journal · 2025Review
- Astragaloside IV-PESV facilitates pyroptosis by enhancing palmitoylation of GSDMD protein mediated by ZDHHC1.Naunyn-Schmiedeberg's archives of pharmacology · 2025Article
- Inhibition of STING-induced mitochondrial Drp1/N-GSDMD-mediated MtDNA release alleviates Sepsis-induced lung injury.Cellular and molecular life sciences : CMLS · 2025Article
- Advanced optical microscopy methods forBiophysical reviews · 2025Review
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Authors and funding
8 authors.
Funding
Abstract
Gasdermin D (GSDMD) executes the cell death program of pyroptosis by assembling into oligomers that permeabilize the plasma membrane. Here, by single-molecule imaging, we elucidate the yet unclear mechanism of Gasdermin D pore assembly and the role of cysteine residues in GSDMD oligomerization. We show that GSDMD preassembles at the membrane into dimeric and trimeric building blocks that can either be inserted into the membrane, or further assemble into higher-order oligomers prior to insertion into the membrane. The GSDMD residues Cys39, Cys57, and Cys192 are the only relevant cysteines involved in GSDMD oligomerization. S-palmitoylation of Cys192, combined with the presence of negatively-charged lipids, controls GSDMD membrane targeting. Simultaneous Cys39/57/192-to-alanine (Ala) mutations, but not Ala mutations of Cys192 or the Cys39/57 pair individually, completely abolish GSDMD insertion into artificial membranes as well as into the plasma membrane. Finally, either Cys192 or the Cys39/Cys57 pair are sufficient to enable formation of GSDMD dimers/trimers, but they are all required for functional higher-order oligomer formation. Overall, our study unveils a cooperative role of Cys192 palmitoylation-mediated membrane binding and Cys39/57/192-mediated oligomerization in GSDMD pore assembly. This study supports a model in which Gasdermin D oligomerization relies on a two-step mechanism mediated by specific cysteine residues.
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