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Despite its established roles in other systems, the mechanistic details of S-acylation in plants, particularly its spatiotemporal regulation during plant-virus interactions, remain poorly understood, largely due to the lack of validated enzyme\u2013substrate pairs. Using the geminivirus tomato yellow leaf curl Chuxiong virus (TYLCCxV) as a model, we show that the viral effector C4 undergoes S-palmitoylation at Cys-4, a modification essential for its plasma membrane anchorage and subsequent mediation of viral pathogenesis. NbPAT4, a palmitoyl acyltransferase from\n                    <jats:italic>Nicotiana benthamiana<\/jats:italic>\n                    , catalyzes C4 S-palmitoylation, promoting its membrane localization, protein stability, and viral infection. Conversely, the C4S substitution (C4\n                    <jats:sup>C4S<\/jats:sup>\n                    ) abolishes S-palmitoylation, leading to cytoplasmic redistribution, protein destabilization, and impaired viral pathogenicity. We further identify NbABHD6 as a depalmitoylase that interacts with C4 and catalyzes its S-depalmitoylation, triggering C4 degradation via the 26S proteasome pathway. This study reveals a regulatory axis in plant-geminivirus interactions, identifying NbPAT4 and NbABHD6 as antagonistic enzymes that dynamically regulate the stoichiometry of C4 S-acylation. These findings support a host\u2013pathogen enzymatic tug-of-war model in which competitive S-palmitoylation homeostasis governs viral subcellular trafficking and pathogenicity.\n                  <\/jats:p>","DOI":"10.1007\/s44154-026-00308-2","type":"journal-article","created":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T01:35:27Z","timestamp":1778031327000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Reversible S-palmitoylation of C4 protein encoded by TYLCCxV orchestrates geminiviral pathogenesis"],"prefix":"10.1007","volume":"6","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5673-8472","authenticated-orcid":false,"given":"Yan","family":"Xie","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Min","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xianan","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Junjie","family":"Yan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wanyi","family":"Yang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yiya","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ming","family":"Yang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaowei","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shuai","family":"Fu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xueping","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2026,5,6]]},"reference":[{"issue":"3","key":"308_CR1","doi-asserted-by":"publisher","first-page":"1597","DOI":"10.1104\/pp.112.203968","volume":"160","author":"O Batistic","year":"2012","unstructured":"Batistic O (2012) Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family. 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