{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T20:54:22Z","timestamp":1791924862744,"version":"4.3.4"},"reference-count":66,"publisher":"Portland Press Ltd.","issue":"04","license":[{"start":{"date-parts":[[2025,7,4]],"date-time":"2025-07-04T00:00:00Z","timestamp":1751587200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,8,29]]},"abstract":"<jats:p>Over the past decade, S-acylation has emerged as a crucial regulator of several innate immune signaling pathways, with new insights continually being gained. S-acylation, a reversible post-translational modification, involves the attachment of fatty acyl chains to cysteine residues, influencing protein localization, function, and stability. In this mini-review, we examine the accumulating evidence of the role of S-acylation in regulating nucleotide oligomerization domain (NOD)-like receptors. NOD-like receptor subfamily P3 (NLRP3), a key player in inflammasome formation, undergoes S-acylation at specific cysteine residues, which are essential for its localization to the trans-Golgi network and other organelles. Various zinc finger Asp-His-His-Cys motif-containing (zDHHC) enzymes mediate this modification, with zDHHC5 being particularly important for activation and the ability of NLRP3 to interact with never in mitosis gene A (NIMA)-related protein kinase 7 (NEK7), promoting inflammasome assembly, caspase-1 activation, and pyroptosis. Alternatively, S-acylation by zDHHC12 targets NLRP3 for chaperone-mediated autophagy, preventing excessive inflammation. NOD2, another NLR, requires S-acylation for membrane localization and effective signaling via the NF-\u03baB and mitogen-activated protein kinase pathways in response to peptidoglycan components. Dysregulation of S-acylation in NOD2 is associated with Crohn\u2019s Disease (hypo-acylated) and Blau syndrome\/early-onset sarcoidosis (hyper-acylated). Soluble NOD2 lacking S-acylation is ubiquitinated and eliminated by the autophagic pathway. This review highlights the significance of understanding the S-acylation cycle and its regulatory mechanisms in developing potential therapeutic interventions for related inflammatory diseases. We also discuss unresolved questions regarding the S-acylation of NOD2 and NLRP3, as well as the regulation of S-acylation in general.<\/jats:p>","DOI":"10.1042\/bst20253026","type":"journal-article","created":{"date-parts":[[2025,7,4]],"date-time":"2025-07-04T10:39:59Z","timestamp":1751625599000},"page":"751-761","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Straight A\u2019s: protein S-acylation in the activation and autophagic degradation of NOD-like receptors"],"prefix":"10.1042","volume":"53","author":[{"given":"Noah R.","family":"Martin","sequence":"first","affiliation":[{"name":"1Department of Pathology, Faculty of Medicine, Dalhousie University, Halifax, Nova Scotia, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6508-168X","authenticated-orcid":false,"given":"Gregory D.","family":"Fairn","sequence":"additional","affiliation":[{"name":"1Department of Pathology, Faculty of Medicine, Dalhousie University, Halifax, Nova Scotia, Canada"},{"name":"2Department of Biochemistry and Molecular Biology, Faculty of Medicine, Dalhousie University, Halifax, Nova Scotia, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2025,7,4]]},"reference":[{"key":"2025121604413106300_BST-2025-3026C1","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/ni1153","article-title":"Innate and adaptive immunity: specificities and signaling hierarchies revisited","volume":"6","author":"Vivier","year":"2005","journal-title":"Nat. Immunol."},{"key":"2025121604413106300_BST-2025-3026C2","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/j.cell.2010.01.022","article-title":"Pattern recognition receptors and inflammation","volume":"140","author":"Takeuchi","year":"2010","journal-title":"Cell"},{"key":"2025121604413106300_BST-2025-3026C3","doi-asserted-by":"crossref","first-page":"699563","DOI":"10.3389\/fimmu.2021.699563","article-title":"DAMPs and Innate Immune Training","volume":"12","author":"Jentho","year":"2021","journal-title":"Front. Immunol."},{"key":"2025121604413106300_BST-2025-3026C4","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1038\/s41392-021-00507-5","article-title":"Pyroptosis: mechanisms and diseases","volume":"6","author":"Yu","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"2025121604413106300_BST-2025-3026C5","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.abb.2019.02.008","article-title":"NOD-like receptors and inflammasomes: A review of their canonical and non-canonical signaling pathways","volume":"670","author":"Platnich","year":"2019","journal-title":"Arch. Biochem. Biophys"},{"key":"2025121604413106300_BST-2025-3026C6","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1038\/s41401-020-00603-2","article-title":"NOD-like receptors in autoimmune diseases","volume":"42","author":"Chen","year":"2021","journal-title":"Acta Pharmacol. Sin."},{"key":"2025121604413106300_BST-2025-3026C7","doi-asserted-by":"crossref","first-page":"167309","DOI":"10.1016\/j.jmb.2021.167309","article-title":"Crystal structure of NLRP3 NACHT domain with an inhibitor defines mechanism of inflammasome inhibition","volume":"433","author":"Dekker","year":"2021","journal-title":"J. Mol. Biol."},{"key":"2025121604413106300_BST-2025-3026C8","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1146\/annurev.pathol.4.110807.092239","article-title":"NOD-Like receptors: role in innate immunity and inflammatory disease","volume":"4","author":"Chen","year":"2009","journal-title":"Annu. Rev. Pathol."},{"key":"2025121604413106300_BST-2025-3026C9","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1038\/s41580-024-00700-8","article-title":"Mechanisms and functions of protein S-acylation","volume":"25","author":"Mesquita S.","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2025121604413106300_BST-2025-3026C10","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1126\/science.aau6391","article-title":"Palmitoylation of NOD1 and NOD2 is required for bacterial sensing","volume":"366","author":"Lu","year":"2019","journal-title":"Science"},{"key":"2025121604413106300_BST-2025-3026C11","doi-asserted-by":"crossref","first-page":"734897","DOI":"10.3389\/fcell.2021.734897","article-title":"Potential role of S-Palmitoylation in cancer stem cells of lung adenocarcinoma","volume":"9","author":"Zhang","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"2025121604413106300_BST-2025-3026C12","doi-asserted-by":"crossref","first-page":"107418","DOI":"10.1016\/j.phrs.2024.107418","article-title":"The ZDHHC13\/ZDHHC17 subfamily: from biological functions to therapeutic targets of diseases","volume":"209","author":"Zhang","year":"2024","journal-title":"Pharmacol. Res."},{"key":"2025121604413106300_BST-2025-3026C13","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1111\/febs.15781","article-title":"Protein S-Palmitoylation: advances and challenges in studying a therapeutically important lipid modification","volume":"289","author":"Main","year":"2022","journal-title":"FEBS J."},{"key":"2025121604413106300_BST-2025-3026C14","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1038\/s41587-023-02030-0","article-title":"A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation","volume":"42","author":"Ocasio","year":"2024","journal-title":"Nat. Biotechnol."},{"key":"2025121604413106300_BST-2025-3026C15","doi-asserted-by":"crossref","first-page":"21939","DOI":"10.1074\/jbc.M115.657668","article-title":"Identification of a novel sequence motif recognized by the ankyrin repeat domain of zDHHC17\/13 S-Acyltransferases","volume":"290","author":"Lemonidis","year":"2015","journal-title":"J. Biol. Chem."},{"key":"2025121604413106300_BST-2025-3026C16","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.210026","article-title":"Substrate recruitment by zDHHC protein acyltransferases","volume":"11","author":"Malgapo","year":"2021","journal-title":"Open Biol."},{"key":"2025121604413106300_BST-2025-3026C17","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1016\/S0959-440X(99)00037-8","article-title":"Alpha\/beta hydrolase fold enzymes: the family keeps growing","volume":"9","author":"Nardini","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"key":"2025121604413106300_BST-2025-3026C18","article-title":"Attenuating ABHD17 isoforms augments the S-acylation and function of NOD2 and a subset of Crohn\u2019s disease-associated NOD2 variants","author":"Dixon","year":"2025","journal-title":"bioRxiv"},{"key":"2025121604413106300_BST-2025-3026C19","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abj8633","article-title":"Cln5 represents a new type of cysteine-based S-depalmitoylase linked to neurodegeneration","volume":"8","author":"Luebben","year":"2022","journal-title":"Sci. Adv."},{"key":"2025121604413106300_BST-2025-3026C20","doi-asserted-by":"crossref","first-page":"113679","DOI":"10.1016\/j.celrep.2024.113679","article-title":"Glutathione-dependent depalmitoylation of phospholemman by peroxiredoxin 6","volume":"43","author":"Howie","year":"2024","journal-title":"Cell Rep."},{"key":"2025121604413106300_BST-2025-3026C21","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1042\/BST20160303","article-title":"Targeting the Ras palmitoylation\/depalmitoylation cycle in cancer","volume":"45","author":"Lin","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"2025121604413106300_BST-2025-3026C22","doi-asserted-by":"crossref","first-page":"15776","DOI":"10.1074\/jbc.M006722200","article-title":"Palmitoylation of caveolin-1 in endothelial cells is post-translational but irreversible","volume":"276","author":"Parat","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2025121604413106300_BST-2025-3026C23","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1038\/nmeth.1769","article-title":"Global profiling of dynamic protein palmitoylation","volume":"9","author":"Martin","year":"2012","journal-title":"Nat. Methods"},{"key":"2025121604413106300_BST-2025-3026C24","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.27826","article-title":"Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation cascade","volume":"6","author":"Abrami","year":"2017","journal-title":"Elife"},{"key":"2025121604413106300_BST-2025-3026C25","doi-asserted-by":"crossref","first-page":"661202","DOI":"10.3389\/fimmu.2021.661202","article-title":"Function of Protein S-Palmitoylation in Immunity and Immune-Related Diseases","volume":"12","author":"Zhang","year":"2021","journal-title":"Front. Immunol."},{"key":"2025121604413106300_BST-2025-3026C26","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.immuni.2024.03.012","article-title":"The NLR family of innate immune and cell death sensors","volume":"57","author":"Sundaram","year":"2024","journal-title":"Immunity"},{"key":"2025121604413106300_BST-2025-3026C27","doi-asserted-by":"crossref","DOI":"10.1038\/s41421-020-0167-x","article-title":"Inflammasome activation and regulation: toward a better understanding of complex mechanisms","volume":"6","author":"Zheng","year":"2020","journal-title":"Cell Discov."},{"key":"2025121604413106300_BST-2025-3026C28","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/s41577-019-0165-0","article-title":"The NLRP3 inflammasome: molecular activation and regulation to therapeutics","volume":"19","author":"Swanson","year":"2019","journal-title":"Nat. Rev. Immunol."},{"key":"2025121604413106300_BST-2025-3026C29","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1038\/nrd.2018.97","article-title":"Targeting the NLRP3 inflammasome in inflammatory diseases","volume":"17","author":"Mangan","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"2025121604413106300_BST-2025-3026C30","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1002\/JLB.3MR0720-513R","article-title":"NLRP3 inflammasome priming: a riddle wrapped in a mystery inside an enigma","volume":"108","author":"McKee","year":"2020","journal-title":"J. Leukoc. Biol."},{"key":"2025121604413106300_BST-2025-3026C31","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1038\/s41423-022-00922-w","article-title":"How location and cellular signaling combine to activate the NLRP3 inflammasome","volume":"19","author":"Akbal","year":"2022","journal-title":"Cell. Mol. Immunol."},{"key":"2025121604413106300_BST-2025-3026C32","doi-asserted-by":"crossref","first-page":"114516","DOI":"10.1016\/j.celrep.2024.114516","article-title":"Fatty acid synthesis promotes inflammasome activation through NLRP3 palmitoylation","volume":"43","author":"Leishman","year":"2024","journal-title":"Cell Rep."},{"key":"2025121604413106300_BST-2025-3026C33","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1038\/nature16959","article-title":"NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux","volume":"530","author":"He","year":"2016","journal-title":"Nature"},{"key":"2025121604413106300_BST-2025-3026C34","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1016\/j.it.2022.10.007","article-title":"Humans pIKK-up NLRP3 to skip NEK7","volume":"43","author":"Malireddi","year":"2022","journal-title":"Trends Immunol"},{"key":"2025121604413106300_BST-2025-3026C35","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/s41586-018-0761-3","article-title":"PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation","volume":"564","author":"Chen","year":"2018","journal-title":"Nature"},{"key":"2025121604413106300_BST-2025-3026C36","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2022111389","article-title":"The lysosomal Ragulator complex activates NLRP3 inflammasome in vivo via HDAC6","volume":"42","author":"Tsujimoto","year":"2023","journal-title":"EMBO J"},{"key":"2025121604413106300_BST-2025-3026C37","doi-asserted-by":"crossref","first-page":"114070","DOI":"10.1016\/j.celrep.2024.114070","article-title":"NLRP3 Cys126 palmitoylation by ZDHHC7 promotes inflammasome activation","volume":"43","author":"Yu","year":"2024","journal-title":"Cell Rep"},{"key":"2025121604413106300_BST-2025-3026C38","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1016\/j.molcel.2024.08.001","article-title":"Consecutive palmitoylation and phosphorylation orchestrates NLRP3 membrane trafficking and inflammasome activation","volume":"84","author":"Nie","year":"2024","journal-title":"Mol. Cell"},{"key":"2025121604413106300_BST-2025-3026C39","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.94302.3","article-title":"S-acylation of NLRP3 provides a nigericin sensitive gating mechanism that controls access to the Golgi","volume":"13","author":"Williams","year":"2024","journal-title":"Elife"},{"key":"2025121604413106300_BST-2025-3026C40","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.tibs.2011.01.003","article-title":"DHHC palmitoyl transferases: substrate interactions and (patho)physiology","volume":"36","author":"Greaves","year":"2011","journal-title":"Trends Biochem. Sci."},{"key":"2025121604413106300_BST-2025-3026C41","doi-asserted-by":"crossref","first-page":"114609","DOI":"10.1016\/j.celrep.2024.114609","article-title":"FDA-approved disulfiram inhibits the NLRP3 inflammasome by regulating NLRP3 palmitoylation","volume":"43","author":"Xu","year":"2024","journal-title":"Cell Rep"},{"key":"2025121604413106300_BST-2025-3026C42","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.cbpa.2021.07.002","article-title":"Inhibitors of DHHC family proteins","volume":"65","author":"Lan","year":"2021","journal-title":"Curr. Opin. Chem. Biol"},{"key":"2025121604413106300_BST-2025-3026C43","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.tibs.2022.10.002","article-title":"The NLRP3 inflammasome: activation and regulation","volume":"48","author":"Xu","year":"2023","journal-title":"Trends Biochem. Sci"},{"key":"2025121604413106300_BST-2025-3026C44","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1038\/s41586-019-1295-z","article-title":"Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome","volume":"570","author":"Sharif","year":"2019","journal-title":"Nature New Biol."},{"key":"2025121604413106300_BST-2025-3026C45","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.1016\/j.molcel.2023.11.015","article-title":"ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3-NEK7 interaction and inflammasome activation","volume":"83","author":"Zheng","year":"2023","journal-title":"Mol. Cell"},{"key":"2025121604413106300_BST-2025-3026C46","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.molcel.2022.12.002","article-title":"Palmitoylation prevents sustained inflammation by limiting NLRP3 inflammasome activation through chaperone-mediated autophagy","volume":"83","author":"Wang","year":"2023","journal-title":"Mol. Cell"},{"key":"2025121604413106300_BST-2025-3026C47","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/s41580-018-0001-6","article-title":"The coming of age of chaperone-mediated autophagy","volume":"19","author":"Kaushik","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2025121604413106300_BST-2025-3026C48","doi-asserted-by":"crossref","first-page":"2821","DOI":"10.1080\/15548627.2023.2187957","article-title":"Palmitoylation promotes chaperone-mediated autophagic degradation of NLRP3 to modulate inflammation","volume":"19","author":"Wang","year":"2023","journal-title":"Autophagy"},{"key":"2025121604413106300_BST-2025-3026C49","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.dci.2017.06.012","article-title":"NOD1 is the innate immune receptor for iE-DAP and can activate NF-\u03baB pathway in teleost fish","volume":"76","author":"Bi","year":"2017","journal-title":"Developmental & Comparative Immunology"},{"key":"2025121604413106300_BST-2025-3026C50","doi-asserted-by":"crossref","first-page":"1242659","DOI":"10.3389\/fimmu.2023.1242659","article-title":"Multifaceted roles and regulation of nucleotide-binding oligomerization domain containing proteins","volume":"14","author":"Dixon","year":"2023","journal-title":"Front. Immunol"},{"key":"2025121604413106300_BST-2025-3026C51","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1177\/1753425910394002","article-title":"Mutational analysis of human NOD1 and NOD2 NACHT domains reveals different modes of activation","volume":"18","author":"Zurek","year":"2012","journal-title":"Innate Immun."},{"key":"2025121604413106300_BST-2025-3026C52","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1111\/j.1462-5822.2004.00433.x","article-title":"Muramyldipeptide and diaminopimelic acid-containing desmuramylpeptides in combination with chemically synthesized Toll-like receptor agonists synergistically induced production of interleukin-8 in a NOD2- and NOD1-dependent manner, respectively, in human: Activation of human monocytic cells via NODs","volume":"7","author":"Uehara","year":"2004","journal-title":"Cell. Microbiol."},{"key":"2025121604413106300_BST-2025-3026C53","doi-asserted-by":"crossref","first-page":"10946","DOI":"10.1073\/pnas.1912866117","article-title":"NOD2 modulates immune tolerance via the GM-CSF-dependent generation of CD103+ dendritic cells","volume":"117","author":"Prescott","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2025121604413106300_BST-2025-3026C54","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1002\/path.2271","article-title":"Nod-like proteins in inflammation and disease","volume":"214","author":"Carneiro","year":"2008","journal-title":"J. Pathol."},{"key":"2025121604413106300_BST-2025-3026C55","doi-asserted-by":"crossref","DOI":"10.1002\/eji.202350476","article-title":"S-palmitoylation regulates innate immune signaling pathways: molecular mechanisms and targeted therapies","volume":"53","author":"Cai","year":"2023","journal-title":"Eur. J. Immunol."},{"key":"2025121604413106300_BST-2025-3026C56","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1038\/s41418-022-00942-z","article-title":"Palmitoylation restricts SQSTM1\/p62-mediated autophagic degradation of NOD2 to modulate inflammation","volume":"29","author":"Zhou","year":"2022","journal-title":"Cell Death Differ."},{"key":"2025121604413106300_BST-2025-3026C57","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0041255","article-title":"TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation","volume":"7","author":"Zurek","year":"2012","journal-title":"PLoS ONE"},{"key":"2025121604413106300_BST-2025-3026C58","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2020106272","article-title":"Cellular stress promotes NOD1\/2-dependent inflammation via the endogenous metabolite sphingosine-1-phosphate","volume":"40","author":"Pei","year":"2021","journal-title":"EMBO J"},{"key":"2025121604413106300_BST-2025-3026C59","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1038\/ni.1782","article-title":"Activation of innate immune antiviral responses by Nod2","volume":"10","author":"Sabbah","year":"2009","journal-title":"Nat. Immunol."},{"key":"2025121604413106300_BST-2025-3026C60","doi-asserted-by":"crossref","first-page":"14640","DOI":"10.1074\/jbc.REV120.014717","article-title":"Regulatory effects of post-translational modifications on zDHHC S-acyltransferases","volume":"295","author":"Zmuda","year":"2020","journal-title":"J. Biol. Chem"},{"key":"2025121604413106300_BST-2025-3026C61","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.75804","article-title":"Exploring the expression patterns of palmitoylating and de-palmitoylating enzymes in the mouse brain using the curated RNA-seq database BrainPalmSeq","volume":"11","author":"Wild","year":"2022","journal-title":"Elife"},{"key":"2025121604413106300_BST-2025-3026C62","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-023-43027-2","article-title":"SARS-CoV-2 hijacks a cell damage response, which induces transcription of a more efficient Spike S-acyltransferase","volume":"14","author":"S Mesquita","year":"2023","journal-title":"Nat. Commun."},{"key":"2025121604413106300_BST-2025-3026C63","article-title":"Functional Dissection of the Zdhhc5-GOLGA7 Protein Palmitoylation Complex","author":"Kahlson","year":"2025","journal-title":"bioRxiv"},{"key":"2025121604413106300_BST-2025-3026C64","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.251819","article-title":"Accessory proteins of the zDHHC family of S-acylation enzymes","volume":"133","author":"Salaun","year":"2020","journal-title":"J. Cell. Sci."},{"key":"2025121604413106300_BST-2025-3026C65","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.260629","article-title":"Activity-dependent post-translational regulation of palmitoylating and depalmitoylating enzymes in the hippocampus","volume":"136","author":"Abazari","year":"2023","journal-title":"J. Cell. Sci."},{"key":"2025121604413106300_BST-2025-3026C66","doi-asserted-by":"crossref","DOI":"10.1038\/s42003-020-01145-3","article-title":"Control of protein palmitoylation by regulating substrate recruitment to a zDHHC-protein acyltransferase","volume":"3","author":"Plain","year":"2020","journal-title":"Commun. Biol."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/53\/04\/751\/975391\/bst-2025-3026.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/53\/04\/751\/975391\/bst-2025-3026.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,12,16]],"date-time":"2025-12-16T09:41:56Z","timestamp":1765878116000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/53\/04\/751\/236294\/Straight-A-s-protein-S-acylation-in-the-activation"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7,4]]},"references-count":66,"journal-issue":{"issue":"04","published-online":{"date-parts":[[2025,7,4]]},"published-print":{"date-parts":[[2025,8,29]]}},"URL":"https:\/\/doi.org\/10.1042\/bst20253026","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2025,8,29]]},"published":{"date-parts":[[2025,7,4]]}}}