{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:43:29Z","timestamp":1792788209572,"version":"4.5.0"},"reference-count":38,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T00:00:00Z","timestamp":1782432000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T00:00:00Z","timestamp":1790899200000},"content-version":"vor","delay-in-days":98,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"name":"Agence Nationale de la Recherche","award":["ANR-20-CE44-0015"],"award-info":[{"award-number":["ANR-20-CE44-0015"]}],"id":[{"id":"https:\/\/ror.org\/00rbzpz17","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Conseil R\u00e9gional de Nouvelle-Aquitaine","award":["2020"],"award-info":[{"award-number":["2020"]}],"id":[{"id":"https:\/\/ror.org\/02mre5m81","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Idex Junior chair","award":["OPE 2019-0436"],"award-info":[{"award-number":["OPE 2019-0436"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Virol J"],"DOI":"10.1186\/s12985-026-03216-z","type":"journal-article","created":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T03:46:24Z","timestamp":1782445584000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["S-palmitoylation of the v-ATPase subunit RNAseK is necessary for Zika virus infection"],"prefix":"10.1186","volume":"23","author":[{"given":"Santiago","family":"Leiva","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Recordon-Pinson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucile","family":"Fischer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-Line","family":"Andreola","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emmanuelle","family":"Thinon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,6,26]]},"reference":[{"key":"3216_CR1","doi-asserted-by":"publisher","first-page":"488","DOI":"10.1038\/s41580-024-00700-8","volume":"25","author":"Francisco S Mesquita","year":"2024","unstructured":"Mesquita FS, Abrami L, Linder M, Bamji SX, Dickinson BC, van der Goot F G . Mechanisms and functions of protein S-acylation. Nat Rev Mol Cell Biol. 2024;25:488\u2013509. https:\/\/doi.org\/10.1038\/s41580-024-00700-8","journal-title":"Nat Rev Mol Cell Biol"},{"key":"3216_CR2","doi-asserted-by":"publisher","unstructured":"Main A, Fuller W. Protein S-Palmitoylation: advances and challenges in studying a therapeutically important lipid modification. FEBS J. 2022;289:861\u201382. https:\/\/doi.org\/10.1111\/febs.15781","DOI":"10.1111\/febs.15781"},{"key":"3216_CR3","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1152\/physrev.00032.2014","volume":"95","author":"LH Chamberlain","year":"2015","unstructured":"Chamberlain LH, Shipston MJ. The physiology of protein S-acylation. Physiol Rev. 2015;95:341\u201376. https:\/\/doi.org\/10.1152\/physrev.00032.2014.","journal-title":"Physiol Rev"},{"key":"3216_CR4","doi-asserted-by":"publisher","unstructured":"Zhang N, Zhao H, Zhang L. Fatty Acid Synthase Promotes the Palmitoylation of Chikungunya Virus nsP1. J Virol. 2019;93. https:\/\/doi.org\/10.1128\/jvi.01747-18.","DOI":"10.1128\/jvi.01747-18"},{"key":"3216_CR5","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1042\/BST20120210","volume":"41","author":"M Veit","year":"2013","unstructured":"Veit M, Serebryakova MV, Kordyukova LV. Palmitoylation of influenza virus proteins. Biochem Soc Trans. 2013;41:50\u20135. https:\/\/doi.org\/10.1042\/BST20120210.","journal-title":"Biochem Soc Trans"},{"key":"3216_CR6","doi-asserted-by":"publisher","first-page":"e00906","DOI":"10.1128\/JVI.00906-19","volume":"94","author":"M-J Wu","year":"2019","unstructured":"Wu M-J, Shanmugam S, Welsch C, Yi M. Palmitoylation of Hepatitis C Virus NS2 Regulates Its Subcellular Localization and NS2-NS3 Autocleavage. J Virol. 2019;94:e00906\u201319. https:\/\/doi.org\/10.1128\/JVI.00906-19.","journal-title":"J Virol"},{"key":"3216_CR7","doi-asserted-by":"publisher","first-page":"610","DOI":"10.1038\/nchembio.405","volume":"6","author":"JS Yount","year":"2010","unstructured":"Yount JS, Moltedo B, Yang Y-Y, Charron G, Moran TM, L\u00f3pez CB, et al. Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3. Nat Chem Biol. 2010;6:610\u20134. https:\/\/doi.org\/10.1038\/nchembio.405.","journal-title":"Nat Chem Biol"},{"key":"3216_CR8","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1038\/s41589-018-0213-2","volume":"15","author":"JS Spence","year":"2019","unstructured":"Spence JS, He R, Hoffmann H-H, Das T, Thinon E, Rice CM, et al. IFITM3 directly engages and shuttles incoming virus particles to lysosomes. Nat Chem Biol. 2019;15:259\u201368. https:\/\/doi.org\/10.1038\/s41589-018-0213-2.","journal-title":"Nat Chem Biol"},{"key":"3216_CR9","doi-asserted-by":"publisher","first-page":"844","DOI":"10.1021\/acschembio.1c00013","volume":"16","author":"EH Garst","year":"2021","unstructured":"Garst EH, Lee H, Das T, Bhattacharya S, Percher A, Wiewiora R, et al. Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity. ACS Chem Biol. 2021;16:844\u201356. https:\/\/doi.org\/10.1021\/acschembio.1c00013.","journal-title":"ACS Chem Biol"},{"key":"3216_CR10","doi-asserted-by":"publisher","unstructured":"Hackett BA, Yasunaga A, Panda D, Tartell MA, Hopkins KC, Hensley SE et al. RNASEK is required for internalization of diverse acid-dependent viruses. Proceedings of the National Academy of Sciences. 2015;112:7797\u2013802. https:\/\/doi.org\/10.1073\/pnas.1424098112","DOI":"10.1073\/pnas.1424098112"},{"key":"3216_CR11","doi-asserted-by":"publisher","unstructured":"Perreira JM, Aker AM, Savidis G, Chin CR, McDougall WM, Portmann JM, et al. RNASEK Is a V-ATPase-Associated Factor Required for Endocytosis and the Replication of Rhinovirus, Influenza A Virus, and Dengue Virus. Cell Rep. 2015;12:850\u201363. https:\/\/doi.org\/10.1016\/j.celrep.2015.06.076","DOI":"10.1016\/j.celrep.2015.06.076"},{"key":"3216_CR12","doi-asserted-by":"publisher","first-page":"7743","DOI":"10.1038\/s41467-024-52049-3","volume":"15","author":"AN Makar","year":"2024","unstructured":"Makar AN, Boraman A, Mosen P, Simpson JE, Marques J, Michelberger T, et al. The V-ATPase complex component RNAseK is required for lysosomal hydrolase delivery and autophagosome degradation. Nat Commun. 2024;15:7743. https:\/\/doi.org\/10.1038\/s41467-024-52049-3.","journal-title":"Nat Commun"},{"key":"3216_CR13","doi-asserted-by":"publisher","first-page":"1240","DOI":"10.1126\/science.aaz2924","volume":"367","author":"YM Abbas","year":"2020","unstructured":"Abbas YM, Wu D, Bueler SA, Robinson CV, Rubinstein JL. Structure of V-ATPase from the mammalian brain. Science. 2020;367:1240\u20136. https:\/\/doi.org\/10.1126\/science.aaz2924.","journal-title":"Science"},{"key":"3216_CR14","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1016\/j.tibs.2019.12.007","volume":"45","author":"T Vasanthakumar","year":"2020","unstructured":"Vasanthakumar T, Rubinstein JL. Structure and Roles of V-type ATPases. Trends Biochem Sci. 2020;45:295\u2013307. https:\/\/doi.org\/10.1016\/j.tibs.2019.12.007.","journal-title":"Trends Biochem Sci"},{"key":"3216_CR15","doi-asserted-by":"publisher","first-page":"160","DOI":"10.3390\/v3020160","volume":"3","author":"JM Smit","year":"2011","unstructured":"Smit JM, Moesker B, Rodenhuis-Zybert I, Wilschut J. Flavivirus cell entry and membrane fusion. Viruses. 2011;3:160\u201371. https:\/\/doi.org\/10.3390\/v3020160.","journal-title":"Viruses"},{"key":"3216_CR16","doi-asserted-by":"publisher","first-page":"1830","DOI":"10.1126\/science.1153263","volume":"319","author":"L Li","year":"2008","unstructured":"Li L, Lok S-M, Yu I-M, Zhang Y, Kuhn RJ, Chen J, et al. The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science. 2008;319:1830\u20134. https:\/\/doi.org\/10.1126\/science.1153263.","journal-title":"Science"},{"key":"3216_CR17","doi-asserted-by":"publisher","first-page":"1782","DOI":"10.1038\/s41467-021-22111-5","volume":"12","author":"R Wang","year":"2021","unstructured":"Wang R, Wang J, Hassan A, Lee C-H, Xie X-S, Li X. Molecular basis of V-ATPase inhibition by bafilomycin A1. Nat Commun. 2021;12:1782. https:\/\/doi.org\/10.1038\/s41467-021-22111-5.","journal-title":"Nat Commun"},{"key":"3216_CR18","doi-asserted-by":"publisher","first-page":"e71332","DOI":"10.1096\/fj.202503348RR","volume":"39","author":"M Wan","year":"2025","unstructured":"Wan M, Zhu Y, Dong J, Kang J, Fang Y, Zhou B, et al. Loss of RNASEK Terminates Egg Cylinder Development by Impairing Lysosomal Function Associated With V-ATPase in Mouse. FASEB J. 2025;39:e71332. https:\/\/doi.org\/10.1096\/fj.202503348RR.","journal-title":"FASEB J"},{"key":"3216_CR19","doi-asserted-by":"publisher","first-page":"14612","DOI":"10.1038\/ncomms14612","volume":"8","author":"MB Bagh","year":"2017","unstructured":"Bagh MB, Peng S, Chandra G, Zhang Z, Singh SP, Pattabiraman N, et al. Misrouting of v-ATPase subunit V0a1 dysregulates lysosomal acidification in a neurodegenerative lysosomal storage disease model. Nat Commun. 2017;8:14612. https:\/\/doi.org\/10.1038\/ncomms14612.","journal-title":"Nat Commun"},{"key":"3216_CR20","doi-asserted-by":"publisher","first-page":"1907","DOI":"10.1021\/acs.jproteome.8b00002","volume":"17","author":"E Thinon","year":"2018","unstructured":"Thinon E, Fernandez JP, Molina HH, Hang HC. Selective enrichment and direct analysis of protein S-palmitoylation sites. J Proteome Res. 2018;17:1907\u201322. https:\/\/doi.org\/10.1021\/acs.jproteome.8b00002.","journal-title":"J Proteome Res"},{"key":"3216_CR21","doi-asserted-by":"publisher","first-page":"1800","DOI":"10.1002\/cbic.201600213","volume":"17","author":"E Thinon","year":"2016","unstructured":"Thinon E, Percher A, Hang HC. Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins. ChemBioChem. 2016;17:1800\u20133. https:\/\/doi.org\/10.1002\/cbic.201600213.","journal-title":"ChemBioChem"},{"key":"3216_CR22","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1021\/acschembio.5c00824","volume":"21","author":"C Freyermuth","year":"2026","unstructured":"Freyermuth C, Dupuy J-W, Renault TT, Claverol S, Raymond A-A, Thinon E. A Chemical Proteomics Method to Quantify Cysteine S-Acylation. ACS Chem Biol. 2026;21:312\u201325. https:\/\/doi.org\/10.1021\/acschembio.5c00824.","journal-title":"ACS Chem Biol"},{"key":"3216_CR23","doi-asserted-by":"publisher","first-page":"524","DOI":"10.3390\/v11060524","volume":"11","author":"C Sabino","year":"2019","unstructured":"Sabino C, Basic M, Bender D, Elgner F, Himmelsbach K, Hildt E. Bafilomycin A1 and U18666A Efficiently Impair ZIKV Infection. Viruses. 2019;11:524. https:\/\/doi.org\/10.3390\/v11060524.","journal-title":"Viruses"},{"key":"3216_CR24","doi-asserted-by":"publisher","first-page":"242","DOI":"10.3389\/fmicb.2020.00242","volume":"11","author":"M Li","year":"2020","unstructured":"Li M, Zhang D, Li C, Zheng Z, Fu M, Ni F, et al. Characterization of Zika Virus Endocytic Pathways in Human Glioblastoma Cells. Front Microbiol. 2020;11:242. https:\/\/doi.org\/10.3389\/fmicb.2020.00242.","journal-title":"Front Microbiol"},{"key":"3216_CR25","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1093\/oxfordjournals.aje.a118408","volume":"27","author":"LJ Reed","year":"1938","unstructured":"Reed LJ, Muench H. Simple method of estimating fifty per cent endpoints. Am J Epidemiol. 1938;27:493\u20137.","journal-title":"Am J Epidemiol"},{"key":"3216_CR26","doi-asserted-by":"publisher","first-page":"132","DOI":"10.3390\/pathogens14020132","volume":"14","author":"Y Jang","year":"2025","unstructured":"Jang Y, Bunz F. Dynamic Modulation of IRE1\u03b1-XBP1 Signaling by Adenovirus. Pathogens. 2025;14:132. https:\/\/doi.org\/10.3390\/pathogens14020132.","journal-title":"Pathogens"},{"key":"3216_CR27","doi-asserted-by":"publisher","first-page":"eadd8910","DOI":"10.1126\/sciadv.add8910","volume":"9","author":"D Zenko","year":"2023","unstructured":"Zenko D, Marsh J, Castle AR, Lewin R, Fischer R, Tofaris GK. Monitoring \u03b1-synuclein ubiquitination dynamics reveals key endosomal effectors mediating its trafficking and degradation. Sci Adv. 2023;9:eadd8910. https:\/\/doi.org\/10.1126\/sciadv.add8910.","journal-title":"Sci Adv"},{"key":"3216_CR28","doi-asserted-by":"publisher","unstructured":"Schymkowitz J, Borg J, Stricher F, Nys R, Rousseau F, Serrano L. The FoldX web server: an online force field. Nucleic Acids Res. 2005;382\u20138. https:\/\/doi.org\/10.1093\/nar\/gki387","DOI":"10.1093\/nar\/gki387"},{"key":"3216_CR29","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1016\/j.jmb.2004.01.002","volume":"336","author":"J Khatun","year":"2004","unstructured":"Khatun J, Khare SD, Dokholyan NV. Can contact potentials reliably predict stability of proteins? J Mol Biol. 2004;336:1223\u201338. https:\/\/doi.org\/10.1016\/j.jmb.2004.01.002.","journal-title":"J Mol Biol"},{"key":"3216_CR30","doi-asserted-by":"publisher","unstructured":"Percher A, Ramakrishnan S, Thinon E, Yuan X, Yount JS, Hang HC. Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation. Proceedings of the National Academy of Sciences. 2016;113:4302\u20137. https:\/\/doi.org\/10.1073\/pnas.1602244113","DOI":"10.1073\/pnas.1602244113"},{"key":"3216_CR31","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1042\/BST20150004","volume":"43","author":"E Thinon","year":"2015","unstructured":"Thinon E, Hang HC. Chemical reporters for exploring protein acylation. Biochem Soc Trans. 2015;43:253\u201361. https:\/\/doi.org\/10.1042\/BST20150004.","journal-title":"Biochem Soc Trans"},{"key":"3216_CR32","doi-asserted-by":"publisher","unstructured":"Raj N, Greune L, Kahms M, Mildner K, Franzkoch R, Psathaki OE, et al. Early Endosomes Act as Local Exocytosis Hubs to Repair Endothelial Membrane Damage. Adv Sci. 2023;10:e2300244. https:\/\/doi.org\/10.1002\/advs.202300244","DOI":"10.1002\/advs.202300244"},{"key":"3216_CR33","doi-asserted-by":"publisher","first-page":"210390","DOI":"10.1098\/rsob.210390","volume":"12","author":"R Elliot Murphy","year":"2022","unstructured":"Elliot Murphy R, Banerjee A. In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases. Open Biol. 2022;12:210390. https:\/\/doi.org\/10.1098\/rsob.210390.","journal-title":"Open Biol"},{"key":"3216_CR34","doi-asserted-by":"publisher","first-page":"388","DOI":"10.1016\/j.bbrc.2013.04.001","volume":"434","author":"C Kong","year":"2013","unstructured":"Kong C, Lange JJ, Samovski D, Su X, Liu J, Sundaresan S, et al. Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation. Biochem Biophys Res Commun. 2013;434:388\u201393. https:\/\/doi.org\/10.1016\/j.bbrc.2013.04.001.","journal-title":"Biochem Biophys Res Commun"},{"key":"3216_CR35","doi-asserted-by":"publisher","first-page":"e0038223","DOI":"10.1128\/jvi.00382-23","volume":"97","author":"X Ma","year":"2023","unstructured":"Ma X, Xia Q, Liu K, Wu Z, Li C, Xiao C, et al. Palmitoylation at Residue C221 of Japanese Encephalitis Virus NS2A Protein Contributes to Viral Replication Efficiency and Virulence. J Virol. 2023;97:e0038223. https:\/\/doi.org\/10.1128\/jvi.00382-23.","journal-title":"J Virol"},{"key":"3216_CR36","doi-asserted-by":"publisher","first-page":"e0176024","DOI":"10.1128\/jvi.01760-24","volume":"99","author":"W Qin","year":"2025","unstructured":"Qin W, Kong N, Xie S, Liu H, Yang X, Wang Y, et al. RNASEK interacting with PEDV structural proteins facilitates virus entry via clathrin-mediated endocytosis. J Virol. 2025;99:e0176024. https:\/\/doi.org\/10.1128\/jvi.01760-24.","journal-title":"J Virol"},{"key":"3216_CR37","doi-asserted-by":"publisher","first-page":"1546","DOI":"10.1021\/acschembio.1c00405","volume":"16","author":"S-A Azizi","year":"2021","unstructured":"Azizi S-A, Lan T, Delalande C, Kathayat RS, Mejia FB, Qin A, et al. Development of an Acrylamide-Based Inhibitor of Protein S-Acylation. ACS Chem Biol. 2021;16:1546\u201356. https:\/\/doi.org\/10.1021\/acschembio.1c00405.","journal-title":"ACS Chem Biol"},{"key":"3216_CR38","doi-asserted-by":"publisher","first-page":"1445","DOI":"10.1038\/s41467-025-56716-x","volume":"16","author":"C-W Kuo","year":"2025","unstructured":"Kuo C-W, G\u00f6k C, Fulton H, Dickson-Murray E, Adu S, Gallen EK, et al. Nanobody-thioesterase chimeras to specifically target protein palmitoylation. Nat Commun. 2025;16:1445. https:\/\/doi.org\/10.1038\/s41467-025-56716-x.","journal-title":"Nat Commun"}],"container-title":["Virology Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s12985-026-03216-z","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12985-026-03216-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12985-026-03216-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T06:32:38Z","timestamp":1790922758000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1186\/s12985-026-03216-z"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,26]]},"references-count":38,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["3216"],"URL":"https:\/\/doi.org\/10.1186\/s12985-026-03216-z","relation":{},"ISSN":["1743-422X"],"issn-type":[{"value":"1743-422X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,26]]},"assertion":[{"value":"1 July 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"1 June 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"26 June 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Not applicable.","order":1,"name":"Ethics","label":"Ethics approval and consent to participate","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"All authors have read and agreed to this submitted version of our manuscript.","order":2,"name":"Ethics","label":"Consent for publication","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"234"}}