title: The E3 Ligase APIP10 Connects the Effector AvrPiz-t to the NLR Receptor Piz-t in Rice.
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.affiliation: 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.
authors.forename: Chan Ho
authors.initials: CH
authors.lastname: Park
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
authors.forename: Gautam
authors.initials: G
authors.lastname: Shirsekar
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
authors.forename: Maria
authors.initials: M
authors.lastname: Bellizzi
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.|Biotechnology Research Institute, Fujian Academy of Agricultural Sciences, Fuzhou, Fujian, China.
authors.forename: Songbiao
authors.initials: S
authors.lastname: Chen
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
authors.forename: Pattavipha
authors.initials: P
authors.lastname: Songkumarn
authors.affiliation: State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
authors.forename: Xin
authors.initials: X
authors.lastname: Xie
authors.affiliation: State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
authors.forename: Xuetao
authors.initials: X
authors.lastname: Shi
authors.affiliation: State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.
authors.forename: Yuese
authors.initials: Y
authors.lastname: Ning
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
authors.forename: Bo
authors.initials: B
authors.lastname: Zhou
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
authors.forename: Pavinee
authors.initials: P
authors.lastname: Suttiviriya
authors.affiliation: Department of Plant Pathology, Ohio State University, Columbus, Ohio, United States of America.
authors.forename: Mo
authors.initials: M
authors.lastname: Wang
authors.affiliation: Meiji Seika Kaisha Ltd, Health & Bioscience Laboratories, Tokyo, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Umemura
authors.affiliation: 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.
authors.forename: Guo-Liang
authors.initials: GL
authors.lastname: Wang
mesh_terms: D020082:Magnaporthe; D012275:Oryza / Q000201:enzymology / Q000382:microbiology*; D010935:Plant Diseases / Q000382:microbiology*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination / Q000276:immunology
chemical_list: D044767:Ubiquitin-Protein Ligases