A fungal core effector exploits the OsPUX8B.2-OsCDC48-6 module to suppress plant immunity

文献类型： 外文期刊

第一作者： Shi, Xuetao

作者： Shi, Xuetao;Xie, Xin;Guo, Yuanwen;Zhang, Junqi;Gong, Ziwen;Zhang, Kai;Mei, Jie;Xia, Xinyao;Xia, Haoxue;Ning, Na;Yang, Qing;Liu, Wende;Shi, Xuetao;Gong, Ziwen;Mei, Jie;Xiao, Yutao;Wang, Guo-Liang

作者机构：

期刊名称：NATURE COMMUNICATIONS （ 影响因子：14.7； 五年影响因子：16.1 ）

ISSN：

年卷期： 2024 年 15 卷 1 期

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收录情况： SCI

摘要： Proteins containing a ubiquitin regulatory X (UBX) domain are cofactors of Cell Division Cycle 48 (CDC48) and function in protein quality control. However, whether and how UBX-containing proteins participate in host-microbe interactions remain unclear. Here we show that MoNLE1, an effector from the fungal pathogen Magnaporthe oryzae, is a core virulence factor that suppresses rice immunity by specifically interfering with OsPUX8B.2. The UBX domain of OsPUX8B.2 is required for its binding to OsATG8 and OsCDC48-6 and controls its 26 S proteasome-dependent stability. OsPUX8B.2 and OsCDC48-6 positively regulate plant immunity against blast fungus, while the high-temperature tolerance heat-shock protein OsBHT, a putative cytoplasmic substrate of OsPUX8B.2-OsCDC48-6, negatively regulates defense against blast infection. MoNLE1 promotes the nuclear migration and degradation of OsPUX8B.2 and disturbs its association with OsBHT. Given the high conservation of MoNLE1 among fungal isolates, plants with broad and durable blast resistance might be generated by engineering intracellular proteins resistant to MoNLE1. Plant ubiquitin regulatory domain-containing proteins (PUX) play vital roles in CDC48-mediated protein quality control processes. Here Shi et al. show that a conserved core Magnaporthe oryzae effector (MoNLE1) can specially target the rice PUX protein OsPUX8B.2 and interfere with host immune responses.

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