Park Chan Ho, Shirsekar Gautam, Bellizzi Maria, Chen Songbiao, Songkumarn Pattavipha, Xie Xin, Shi Xuetao, Ning Yuese, Zhou Bo, Suttiviriya Pavinee, Wang Mo, Umemura Kenji, Wang Guo-Liang
Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
PLoS Pathog. 2016 Mar 31;12(3):e1005529. doi: 10.1371/journal.ppat.1005529. eCollection 2016 Mar.
Although nucleotide-binding domain, leucine-rich repeat (NLR) proteins are the major immune receptors in plants, the mechanism that controls their activation and immune signaling remains elusive. Here, we report that the avirulence effector AvrPiz-t from Magnaporthe oryzae targets the rice E3 ligase APIP10 for degradation, but that APIP10, in return, ubiquitinates AvrPiz-t and thereby causes its degradation. Silencing of APIP10 in the non-Piz-t background compromises the basal defense against M. oryzae. Conversely, silencing of APIP10 in the Piz-t background causes cell death, significant accumulation of Piz-t, and enhanced resistance to M. oryzae, suggesting that APIP10 is a negative regulator of Piz-t. We show that APIP10 promotes degradation of Piz-t via the 26S proteasome system. Furthermore, we demonstrate that AvrPiz-t stabilizes Piz-t during M. oryzae infection. Together, our results show that APIP10 is a novel E3 ligase that functionally connects the fungal effector AvrPiz-t to its NLR receptor Piz-t in rice.
尽管核苷酸结合结构域富含亮氨酸重复序列（NLR）蛋白是植物中的主要免疫受体，但其激活和免疫信号传导的控制机制仍不清楚。在这里，我们报告来自稻瘟病菌的无毒效应子AvrPiz-t靶向水稻E3连接酶APIP10进行降解，但APIP10反过来使AvrPiz-t泛素化，从而导致其降解。在非Piz-t背景中沉默APIP10会损害对稻瘟病菌的基础防御。相反，在Piz-t背景中沉默APIP10会导致细胞死亡、Piz-t大量积累以及对稻瘟病菌的抗性增强，这表明APIP10是Piz-t的负调节因子。我们表明APIP10通过26S蛋白酶体系统促进Piz-t的降解。此外，我们证明在稻瘟病菌感染期间AvrPiz-t使Piz-t稳定。总之，我们的结果表明APIP10是一种新型E3连接酶，在功能上把真菌效应子AvrPiz-t与其在水稻中的NLR受体Piz-t联系起来。
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