SH3P2, an SH3 domain-containing protein that interacts with both Pib and AvrPib, suppresses effector-triggered, Pib-mediated immunity in rice
文献类型： 外文期刊
作者： Xie, Yunjie 1 ; Wang, Yupeng 1 ; Yu, Xiangzhen 1 ; Lin, Yuelong 1 ; Zhu, Yongsheng 2 ; Chen, Jinwen 2 ; Xie, Hongguang 2 ; Zhang, Qingqing 1 ; Wang, Lanning 1 ; Wei, Yidong 2 ; Xiao, Yanjia 2 ; Cai, Qiuhua 2 ; Zheng, Yanmei 2 ; Wang, Mo 1 ; Xie, Huaan 1 ; Zhang, Jianfu 1 ;
作者机构： 1.Fujian Agr & Forestry Univ, State Key Lab Ecol Pest Control Fujian & Taiwan Cr, Fuzhou 350002, Peoples R China
2.Fujian Acad Agr Sci, Rice Res Inst, Fuzhou 350018, Peoples R China
3.Minist Agr & Affairs, Key Lab Germplasm Innovat & Mol Breeding Hybrid Ri, Fuzhou, Peoples R China
4.Minist Sci & Technol, Incubator Natl Key Lab Germplasm Innovat & Mol Bre, Fuzhou, Peoples R China
5.Natl Rice Improvement Ctr China, Fuzhou Branch, Fuzhou, Peoples R China
6.Fujian Engn Lab Crop Mol Breeding, Fuzhou, Peoples R China
7.Fujian Key Lab Rice Mol Breeding, Fuzhou 350003, Peoples R China
关键词： rice; blast fungus; Pib-AvrPib recognition; SH3 domain-containing protein; protector
期刊名称：MOLECULAR PLANT （ 影响因子：21.949； 五年影响因子：19.617 ）
ISSN： 1674-2052
年卷期： 2022 年 15 卷 12 期
页码：
收录情况： SCI
摘要： Plants usually keep resistance (R) proteins in a static state under normal conditions to avoid autoimmu-nity and save energy for growth, but R proteins can be rapidly activated upon perceiving pathogen inva-sion. Pib, the first cloned blast disease R gene in rice, encoding a nucleotide-binding leucine-rich repeat (NLR) protein, mediates resistance to the blast fungal (Magnaporthe oryzae) isolates carrying the aviru-lence gene AvrPib. However, the molecular mechanisms about how Pib recognizes AvrPib and how it is inactivated and activated remain largely unclear. In this study, through map-based cloning and CRISPR-Cas9 gene editing, we proved that Pib contributes to the blast disease resistance of rice cultivar Yunyin (YY). Furthermore, an SH3 domain-containing protein, SH3P2, was found to associate with Pib mainly at clathrin-coated vesicles in rice cells, via direct binding with the coiled-coil (CC) domain of Pib. Inter-estingly, overexpression of SH3P2 in YY compromised Pib-mediated resistance to M. oryzae isolates carrying AvrPib and Pib-AvrPib recognition-induced cell death. SH3P2 competitively inhibits the self -association of the Pib CC domain in vitro, suggesting that binding of SH3P2 with Pib undermines its homodimerization. Moreover, SH3P2 can also interact with AvrPib and displays higher affinity to AvrPib than to Pib, which leads to dissociation of SH3P2 from Pib in the presence of AvrPib. Taken together, our results suggest that SH3P2 functions as a "protector"to keep Pib in a static state by direct interaction during normal growth but could be triggered off by the invasion of AvrPib-carrying M. oryzae isolates. Our study reveals a new mechanism about how an NLR protein is inactivated under normal con-ditions but is activated upon pathogen infection.
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