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New Phytol. 2018 Oct;220(1):163-177. doi: 10.1111/nph.15279. Epub 2018 Jun 22.

EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis.

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Division of Applied Life Sciences (BK21+) and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju, 52828, Korea.
Department of Biomedical Science and Engineering, Konkuk University, Seoul, 05029, Korea.


Investigation of the endoplasmic reticulum-associated degradation (ERAD) system in plants led to the identification of ERAD-mediating RING finger protein (EMR) as a plant-specific ERAD E3 ligase from Arabidopsis. EMR was significantly up-regulated under endoplasmic reticulum (ER) stress conditions. The EMR protein purified from bacteria displayed high E3 ligase activity, and tobacco leaf-produced EMR mediated mildew resistance locus O-12 (MLO12) degradation in a proteasome-dependent manner. Subcellular localization and coimmunoprecipitation analyses showed that EMR forms a complex with ubiquitin-conjugating enzyme 32 (UBC32) as a cytosolic interaction partner. Mutation of EMR and RNA interference (RNAi) increased the tolerance of plants to ER stress. EMR RNAi in the bri1-5 background led to partial recovery of the brassinosteroid (BR)-insensitive phenotypes as compared with the original mutant plants and increased ER stress tolerance. The presented results suggest that EMR is involved in the plant ERAD system that affects BR signaling under ER stress conditions as a novel Arabidopsis ring finger E3 ligase mainly present in cytosol while the previously identified ERAD E3 components are typically membrane-bound proteins.


Arabidopsis thaliana ; E3 ligase; brassinosteroid (BR) signaling; endoplasmic reticulum (ER) stress; endoplasmic reticulum-associated degradation (ERAD); misfolded proteins


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