PLoS Pathogens | |
The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice | |
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 | |
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【 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
【 预 览 】
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