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The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice.
PLoS Pathog. 2016 Mar; 12(3):e1005529.PP

Abstract

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.

Authors+Show Affiliations

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.Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America. 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.State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.Meiji Seika Kaisha Ltd, Health & Bioscience Laboratories, Tokyo, Japan.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.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

27031246

Citation

Park, Chan Ho, et al. "The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice." PLoS Pathogens, vol. 12, no. 3, 2016, pp. e1005529.
Park CH, Shirsekar G, Bellizzi M, et al. The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice. PLoS Pathog. 2016;12(3):e1005529.
Park, C. H., Shirsekar, G., Bellizzi, M., Chen, S., Songkumarn, P., Xie, X., Shi, X., Ning, Y., Zhou, B., Suttiviriya, P., Wang, M., Umemura, K., & Wang, G. L. (2016). The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice. PLoS Pathogens, 12(3), e1005529. https://doi.org/10.1371/journal.ppat.1005529
Park CH, et al. The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice. PLoS Pathog. 2016;12(3):e1005529. PubMed PMID: 27031246.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice. AU - Park,Chan Ho, AU - Shirsekar,Gautam, AU - Bellizzi,Maria, AU - Chen,Songbiao, AU - Songkumarn,Pattavipha, AU - Xie,Xin, AU - Shi,Xuetao, AU - Ning,Yuese, AU - Zhou,Bo, AU - Suttiviriya,Pavinee, AU - Wang,Mo, AU - Umemura,Kenji, AU - Wang,Guo-Liang, Y1 - 2016/03/31/ PY - 2016/02/08/received PY - 2016/03/05/accepted PY - 2016/4/1/entrez PY - 2016/4/1/pubmed PY - 2016/8/16/medline SP - e1005529 EP - e1005529 JF - PLoS pathogens JO - PLoS Pathog VL - 12 IS - 3 N2 - 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. SN - 1553-7374 UR - https://www.unboundmedicine.com/medline/citation/27031246/The_E3_Ligase_APIP10_Connects_the_Effector_AvrPiz_t_to_the_NLR_Receptor_Piz_t_in_Rice_ L2 - https://dx.plos.org/10.1371/journal.ppat.1005529 DB - PRIME DP - Unbound Medicine ER -