The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice

PLoS Pathogens

Xin Xie¹  Kenji Umemura²  Chan Ho Park²  Songbiao Chen²  Pattavipha Songkumarn²  Xuetao Shi²  Mo Wang²  Maria Bellizzi²  Guo-Liang Wang²  Gautam Shirsekar³  Yuese Ning³  Bo Zhou³  Pavinee Suttiviriya³ 

[1] Biotechnology Research Institute, Fujian Academy of Agricultural Sciences, Fuzhou, Fujian, China;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

关键词: Rice;    Ligases;    RNA interference;    Leaves;    Ubiquitination;    Plant fungal pathogens;    Cell death;    Proteasomes;   

DOI  :  10.1371/journal.ppat.1005529

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

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.

【 授权许可】

CC BY