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 speci...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.展开更多
基金supported by the National Key Research and Development Program of China(2024YFD1400702)the National Natural Science Foundation of China(W2411024)to Xueping Zhou.
文摘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.
