The OsSPK1 OsRac1 RAI1 defense signaling pathway is shared by two distantly related NLR proteins in rice blast resistance
文献类型： 外文期刊
作者： Yu, Minxiang 1 ; Zhou, Zhuangzhi 2 ; Liu, Xue 2 ; Yin, Dedong 2 ; Li, Dayong 2 ; Zhao, Xianfeng 2 ; Li, Xiaobing 2 ; Li, Shengping 1 ; Chen, Renjie 1 ; Lu, Ling 1 ; Yang, Dewei 1 ; Tang, Dingzhong 1 ; Zhu, Lihuang 2 ;
作者机构： 1.Fujian Agr & Forestry Univ, State Key Lab Ecol Control Fujian Taiwan Crop Pes, Minist Educ Genet Breeding & Multiple Utilizat Cr, Key Lab,Plant Immun Ctr, Fuzhou 350002, Fujian, Peoples R China
2.Chinese Acad Sci, State Key Lab Plant Genom, Inst Genet & Dev Biol, Beijing 100101, Peoples R China
3.Chinese Acad Sci, Natl Ctr Plant Gene Res Beijing, Inst Genet & Dev Biol, Beijing 100101, Peoples R China
4.Fujian Acad Agr Sci, Rice Res Inst, Fuzhou 350019, Fujian, Peoples R China
5.Beijing Acad Agr & Forestry Sci, Natl Engn Res Ctr Vegetables, Beijing Vegetable Res Ctr, Beijing 100097, Peoples R China
6.Natl Res Inst Family Planning, Reprod Physiol Lab, Beijing 100081, Peoples R China
期刊名称：PLANT PHYSIOLOGY （ 影响因子：8.005； 五年影响因子：9.115 ）
ISSN： 0032-0889
年卷期： 2021 年 187 卷 4 期
页码：
收录情况： SCI
摘要： Resistance (R) proteins are important components of plant innate immunity. Most known R proteins are nucleotide-binding site leucine-rich repeat (NLR) proteins. Although a number of signaling components downstream of NLRs have been identified, we lack a general understanding of the signaling pathways. Here, we used the interaction between rice (Oryza sativa) and Magnaporthe oryzae to study signaling of rice NLRs in response to blast infection. We found that in blast resistance mediated by the NLR PIRICULARIA ORYZAE RESISTANCE IN DIGU 3 (PID3), the guanine nucleotide exchange factor OsSPK1 works downstream of PID3. OsSPK1 activates the small GTPase OsRac1, which in turn transduces the signal to the transcription factor RAC IMMUNITY1 (RAI1). Further investigation revealed that the three signaling components also play important roles in disease resistance mediated by the distantly related NLR protein Pig, suggesting that the OsSPK1-OsRac1-RAI1 signaling pathway could be conserved across rice NLR-induced blast resistance. In addition, we observed changes in RAI1 levels during blast infection, which led to identification of OsRPT2a, a subunit of the 19S regulatory particle of the 26S proteasome. OsRPT2a seemed to be responsible for RAI1 turnover in a 26S proteasome-dependent manner. Collectively, our results suggest a defense signaling route that might be common to NLR proteins in response to blast infection.
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