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ROS-dependent S-palmitoylation activates cleaved and intact gasdermin D
Gasdermin D (GSDMD) is the common effector for cytokine secretion and pyroptosis downstream of inflammasome activation and was previously shown to form large transmembrane pores after cleavage by inflammatory caspases to generate the GSDMD N-terminal domain (GSDMD-NT) . Here we report that GSDMD Cys...
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| Published in: | Nature (London) 2024-06, Vol.630 (8016), p.437-4 |
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| creator | Du, Gang Healy, Liam B David, Liron Walker, Caitlin El-Baba, Tarick J Lutomski, Corinne A Goh, Byoungsook Gu, Bowen Pi, Xiong Devant, Pascal Fontana, Pietro Dong, Ying Ma, Xiyu Miao, Rui Balasubramanian, Arumugam Puthenveetil, Robbins Banerjee, Anirban Luo, Hongbo R Kagan, Jonathan C Oh, Sungwhan F Robinson, Carol V Lieberman, Judy Wu, Hao |
| description | Gasdermin D (GSDMD) is the common effector for cytokine secretion and pyroptosis downstream of inflammasome activation and was previously shown to form large transmembrane pores after cleavage by inflammatory caspases to generate the GSDMD N-terminal domain (GSDMD-NT)
. Here we report that GSDMD Cys191 is S-palmitoylated and that palmitoylation is required for pore formation. S-palmitoylation, which does not affect GSDMD cleavage, is augmented by mitochondria-generated reactive oxygen species (ROS). Cleavage-deficient GSDMD (D275A) is also palmitoylated after inflammasome stimulation or treatment with ROS activators and causes pyroptosis, although less efficiently than palmitoylated GSDMD-NT. Palmitoylated, but not unpalmitoylated, full-length GSDMD induces liposome leakage and forms a pore similar in structure to GSDMD-NT pores shown by cryogenic electron microscopy. ZDHHC5 and ZDHHC9 are the major palmitoyltransferases that mediate GSDMD palmitoylation, and their expression is upregulated by inflammasome activation and ROS. The other human gasdermins are also palmitoylated at their N termini. These data challenge the concept that cleavage is the only trigger for GSDMD activation. They suggest that reversible palmitoylation is a checkpoint for pore formation by both GSDMD-NT and intact GSDMD that functions as a general switch for the activation of this pore-forming family. |
| doi_str_mv | 10.1038/s41586-024-07373-5 |
| format | article |
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. Here we report that GSDMD Cys191 is S-palmitoylated and that palmitoylation is required for pore formation. S-palmitoylation, which does not affect GSDMD cleavage, is augmented by mitochondria-generated reactive oxygen species (ROS). Cleavage-deficient GSDMD (D275A) is also palmitoylated after inflammasome stimulation or treatment with ROS activators and causes pyroptosis, although less efficiently than palmitoylated GSDMD-NT. Palmitoylated, but not unpalmitoylated, full-length GSDMD induces liposome leakage and forms a pore similar in structure to GSDMD-NT pores shown by cryogenic electron microscopy. ZDHHC5 and ZDHHC9 are the major palmitoyltransferases that mediate GSDMD palmitoylation, and their expression is upregulated by inflammasome activation and ROS. The other human gasdermins are also palmitoylated at their N termini. These data challenge the concept that cleavage is the only trigger for GSDMD activation. They suggest that reversible palmitoylation is a checkpoint for pore formation by both GSDMD-NT and intact GSDMD that functions as a general switch for the activation of this pore-forming family.</description><identifier>ISSN: 0028-0836</identifier><identifier>ISSN: 1476-4687</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/s41586-024-07373-5</identifier><identifier>PMID: 38599239</identifier><language>eng</language><publisher>England: Nature Publishing Group</publisher><subject>Cell death ; Cleavage ; Electron microscopy ; Inflammasomes ; Inflammation ; Localization ; Microscopy ; Palmitoylation ; Polyethylene glycol ; Pore formation ; Pores ; Pyroptosis ; Reactive oxygen species</subject><ispartof>Nature (London), 2024-06, Vol.630 (8016), p.437-4</ispartof><rights>2024. The Author(s), under exclusive licence to Springer Nature Limited.</rights><rights>Copyright Nature Publishing Group Jun 13, 2024</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c331t-7263f3bd46b19b7d0dac95cac5e1981dc2622c803beab395b884b5c78c93a79a3</citedby><cites>FETCH-LOGICAL-c331t-7263f3bd46b19b7d0dac95cac5e1981dc2622c803beab395b884b5c78c93a79a3</cites><orcidid>0000-0001-7509-103X ; 0000-0001-7829-5505 ; 0000-0002-6200-4715 ; 0000-0003-2629-9963 ; 0000-0003-0977-8276 ; 0000-0002-7894-7259 ; 0000-0002-8545-0451 ; 0000-0002-0280-7903 ; 0000-0002-7281-8579 ; 0000-0003-3215-3784 ; 0000-0003-0805-4778 ; 0000-0002-9750-543X ; 0000-0002-7333-8542 ; 0000-0001-8835-6914 ; 0000-0002-2640-1596 ; 0000-0001-9743-6764 ; 0000-0003-2364-2746 ; 0000-0003-4497-9938 ; 0000-0003-1494-6801</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38599239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Du, Gang</creatorcontrib><creatorcontrib>Healy, Liam B</creatorcontrib><creatorcontrib>David, Liron</creatorcontrib><creatorcontrib>Walker, Caitlin</creatorcontrib><creatorcontrib>El-Baba, Tarick J</creatorcontrib><creatorcontrib>Lutomski, Corinne A</creatorcontrib><creatorcontrib>Goh, Byoungsook</creatorcontrib><creatorcontrib>Gu, Bowen</creatorcontrib><creatorcontrib>Pi, Xiong</creatorcontrib><creatorcontrib>Devant, Pascal</creatorcontrib><creatorcontrib>Fontana, Pietro</creatorcontrib><creatorcontrib>Dong, Ying</creatorcontrib><creatorcontrib>Ma, Xiyu</creatorcontrib><creatorcontrib>Miao, Rui</creatorcontrib><creatorcontrib>Balasubramanian, Arumugam</creatorcontrib><creatorcontrib>Puthenveetil, Robbins</creatorcontrib><creatorcontrib>Banerjee, Anirban</creatorcontrib><creatorcontrib>Luo, Hongbo R</creatorcontrib><creatorcontrib>Kagan, Jonathan C</creatorcontrib><creatorcontrib>Oh, Sungwhan F</creatorcontrib><creatorcontrib>Robinson, Carol V</creatorcontrib><creatorcontrib>Lieberman, Judy</creatorcontrib><creatorcontrib>Wu, Hao</creatorcontrib><title>ROS-dependent S-palmitoylation activates cleaved and intact gasdermin D</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>Gasdermin D (GSDMD) is the common effector for cytokine secretion and pyroptosis downstream of inflammasome activation and was previously shown to form large transmembrane pores after cleavage by inflammatory caspases to generate the GSDMD N-terminal domain (GSDMD-NT)
. Here we report that GSDMD Cys191 is S-palmitoylated and that palmitoylation is required for pore formation. S-palmitoylation, which does not affect GSDMD cleavage, is augmented by mitochondria-generated reactive oxygen species (ROS). Cleavage-deficient GSDMD (D275A) is also palmitoylated after inflammasome stimulation or treatment with ROS activators and causes pyroptosis, although less efficiently than palmitoylated GSDMD-NT. Palmitoylated, but not unpalmitoylated, full-length GSDMD induces liposome leakage and forms a pore similar in structure to GSDMD-NT pores shown by cryogenic electron microscopy. ZDHHC5 and ZDHHC9 are the major palmitoyltransferases that mediate GSDMD palmitoylation, and their expression is upregulated by inflammasome activation and ROS. The other human gasdermins are also palmitoylated at their N termini. These data challenge the concept that cleavage is the only trigger for GSDMD activation. They suggest that reversible palmitoylation is a checkpoint for pore formation by both GSDMD-NT and intact GSDMD that functions as a general switch for the activation of this pore-forming family.</description><subject>Cell death</subject><subject>Cleavage</subject><subject>Electron microscopy</subject><subject>Inflammasomes</subject><subject>Inflammation</subject><subject>Localization</subject><subject>Microscopy</subject><subject>Palmitoylation</subject><subject>Polyethylene glycol</subject><subject>Pore formation</subject><subject>Pores</subject><subject>Pyroptosis</subject><subject>Reactive oxygen 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| ispartof | Nature (London), 2024-06, Vol.630 (8016), p.437-4 |
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| source | Nature Journals |
| subjects | Cell death Cleavage Electron microscopy Inflammasomes Inflammation Localization Microscopy Palmitoylation Polyethylene glycol Pore formation Pores Pyroptosis Reactive oxygen species |
| title | ROS-dependent S-palmitoylation activates cleaved and intact gasdermin D |
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