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<p>Modification&#xa0;of proteins by&#xa0;ubiquitin is a dynamic and reversible process. It is unclear whether rice stripe virus (RSV) can modulate the plant deubiquitination pathway. In this study, we found that RSV infection can specifically upregulate the expression of the deubiquitinase <i>NbUBP16</i>. Further analysis revealed that NbUBP16 stabilizes serine hydroxymethyltrasferase (SHMT1) by binding to NbSHMT1 and removing its polyubiquitination modification mediated by E3 ligase MEL, which inhibits downstream SHMT1-mediated ROS accumulation and thereby facilitates RSV infection. Our findings provide new insights into the molecular arms race between pathogens and plants, demonstrating how a plant virus can undermine plant defenses by hijacking host deubiquitination pathways.</p>

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Upregulation of deubiquitinase UBP16 induced by rice stripe virus infection stabilizes SHMT1 to suppress ROS accumulation and facilitate virus infection in Nicotiana benthamiana

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月26日

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  • Kun Wang,
  • Yaqin Wang,
  • Shuai Fu,
  • Yuchong Tan,
  • Liang Wu,
  • Yi Xu,
  • Jianxiang Wu,
  • Xueping Zhou

摘要

Modification of proteins by ubiquitin is a dynamic and reversible process. It is unclear whether rice stripe virus (RSV) can modulate the plant deubiquitination pathway. In this study, we found that RSV infection can specifically upregulate the expression of the deubiquitinase NbUBP16. Further analysis revealed that NbUBP16 stabilizes serine hydroxymethyltrasferase (SHMT1) by binding to NbSHMT1 and removing its polyubiquitination modification mediated by E3 ligase MEL, which inhibits downstream SHMT1-mediated ROS accumulation and thereby facilitates RSV infection. Our findings provide new insights into the molecular arms race between pathogens and plants, demonstrating how a plant virus can undermine plant defenses by hijacking host deubiquitination pathways.