PUB40 attenuates Phytophthora capsici resistance by destabilizing the MEK2-SIPK/WIPK cascade in Nicotiana benthamiana
文献类型： 外文期刊
作者： Zhang, Yifan 1 ; Wang, Jinghao 1 ; Pi, Lei 1 ; Wang, Nan 1 ; Peng, Hao 3 ; Xu, Guangyuan 1 ; Yin, Zhiyuan 1 ; Dou, Daolong 1 ;
作者机构： 1.China Agr Univ, Coll Plant Protect, Beijing 100193, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing 210095, Peoples R China
3.Agr Res Serv, USDA, San Joaquin Valley Agr Sci Ctr, Parlier, CA 93648 USA
4.Nanjing Agr Univ, Acad Adv Interdisciplinary Studies, Nanjing 210095, Peoples R China
关键词： Phytophthora capsici; E3 ubiquitin ligase; Armadillo repeat; Plant U-box protein; Mitogen-activated protein kinase
期刊名称：PHYTOPATHOLOGY RESEARCH （ 影响因子：3.2； 五年影响因子：3.7 ）
ISSN： 2096-5362
年卷期： 2024 年 6 卷 1 期
页码：
收录情况： SCI
摘要： The mitogen-activated protein kinase (MAPK) cascade MEK2-SIPK/WIPK is essential for immunity in Solanaceae plants. This cascade is tightly controlled to prevent harmful hyperactivation. However, the E3 ubiquitin ligases utilized by plants to reduce MEK2- SIPK/WIPK protein levels remain largely elusive. Here, we confirmed the essential role of Nicotiana benthamiana MEK2-SIPK/WIPK in resistance to the oomycete pathogen Phytophthora capsici. Using tobacco rattle virus (TRV)-based gene silencing, we screened prevalent plant U-box protein (PUB)-type E3 ligases with Armadillo (ARM) repeats to characterize those involved in Phytophthora resistance and MEK2-SIPK/WIPK degradation. We found that pub40 knockdown mutants exhibited significantly enhanced resistance to P. capsici. NbPUB40 was under ubiquitination and proteasomal degradation in planta, with two conserved sites (Cys28 and Val41) in the U-box domain being essential for its activity. NbPUB40 was shown to interact with the whole MEK2-SIPK/WIPK cascade and promote their degradation, the ubiquitination levels of which were also notably reduced in the pub40 mutant. Our results reveal a mechanism in which a PUB E3 ubiquitin ligase negatively regulates plant P. capsici resistance by destabilizing the MEK2-SIPK/WIPK cascade.
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