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

• Published in: PLoS pathogens Vol. 12; no. 3; p. e1005529
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01.03.2016; Public Library of Science (PLoS)
• Subjects: Apoptosis; Biology and Life Sciences; Cell death; Gene expression; Genomes; Health aspects; Infections; Ligases; Magnaporthe; NOD-like receptors; Oryza - enzymology; Oryza - microbiology; Pathogens; Physiological aspects; Plant Diseases - microbiology; Proteins; Research and Analysis Methods; Resistance to control; Rice; Ubiquitin-Protein Ligases - metabolism; Ubiquitination - immunology
• ISSN: 1553-7374; 1553-7366; 1553-7374
• DOI: 10.1371/journal.ppat.1005529

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.