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<p>Cysteine palmitoylation (S-palmitoylation or S-acylation) is a reversible post-translational modification dynamically controlled by opposing enzymes: palmitoyl acyltransferases (PATs) and depalmitoylases. 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–substrate 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 <i>Nicotiana benthamiana</i>, catalyzes C4 S-palmitoylation, promoting its membrane localization, protein stability, and viral infection. Conversely, the C4S substitution (C4<sup>C4S</sup>) 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–pathogen enzymatic tug-of-war model in which competitive S-palmitoylation homeostasis governs viral subcellular trafficking and pathogenicity.</p>

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Reversible S-palmitoylation of C4 protein encoded by TYLCCxV orchestrates geminiviral pathogenesis

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年5月6日

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  • Yan Xie,
  • Min Zhao,
  • Xianan Liu,
  • Junjie Yan,
  • Wanyi Yang,
  • Yiya Chen,
  • Ming Yang,
  • Xiaowei Wang,
  • Shuai Fu,
  • Xueping Zhou

摘要

Cysteine palmitoylation (S-palmitoylation or S-acylation) is a reversible post-translational modification dynamically controlled by opposing enzymes: palmitoyl acyltransferases (PATs) and depalmitoylases. 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–substrate 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 Nicotiana benthamiana, catalyzes C4 S-palmitoylation, promoting its membrane localization, protein stability, and viral infection. Conversely, the C4S substitution (C4C4S) 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–pathogen enzymatic tug-of-war model in which competitive S-palmitoylation homeostasis governs viral subcellular trafficking and pathogenicity.