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

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.

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Publication Details

Journal
Stress Biology
Published
2025-10-26
DOI
https://doi.org/10.1007/s44154-025-00265-2
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
0.00

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article

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

Liang Wu, Shuai Fu, Yung-Chie Tan, Kun Wang et al.
Stress Biology
Ubiquitin and proteasome pathways
article

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

Liang Wu, Shuai Fu, Yung-Chie Tan, Kun Wang, Xueping Zhou, Yaqin Wang, Yi Xu, Jianxiang Wu
article en

Abstract

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.

Stress BiologyVol. 5(1)
Nanjing Agricultural University (CN), Institute of Plant Protection (CN), Chinese Academy of Agricultural Sciences (CN), Zhejiang University of Technology (CN), Zhejiang University (CN)
National Natural Science Foundation of China, National Key Research and Development Program of China
Openalex Percentile: Top 73%
Ubiquitin and proteasome pathways
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