SIMP1 modulates salt tolerance by elevating ERAD efficiency through UMP1A-mediated proteasome maturation in plants
SIMP1 modulates salt tolerance by elevating ERAD efficiency through UMP1A-mediated proteasome maturation in plants
复制标题
SIMP1 通过 UMP1A 介导的植物蛋白酶体成熟提高 ERAD 效率来调节耐盐性
DOI：
10.1111/nph.17628
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发表时间：
2021-08-06
期刊：
影响因子：
9.4
通讯作者：
Zhou, Huapeng
中科院分区：
文献类型：
--
作者：
He, Jiaxian;Zhuang, Yufen;Zhou, Huapeng
Salt stress significantly induces accumulation of misfolded or unfolded proteins in plants. Endoplasmic reticulum (ER)-associated protein degradation (ERAD) and other degradative machineries function in the degradation of these abnormal proteins, leading to enhanced salt tolerance in plants. Here we characterise that a novel receptor-like kinase, Salt-Induced Malectin-like domain-containing Protein1 (SIMP1), elevates ERAD efficiency during salt stress through UMP1A, a putative proteasome maturation factor in Arabidopsis. SIMP1 loss-of-function caused a salt-hypersensitive phenotype. SIMP1 interacts and phosphorylates UMP1A, and the protein stability of UMP1A is positively regulated by SIMP1. SIMP1 modulates the 26S proteasome maturation possibly through enhancing the recruitment of specific beta subunits of the core catalytic particle to UMP1A. Functionally, the SIMP1-UMP1A module plays a positive role in ERAD efficiency in Arabidopsis. The degradation of misfolded/unfolded proteins was impaired in both simp1 and ump1a mutants during salt stress. Consistently, both simp1 and ump1a plants exhibited reduced ER stress tolerance. Phenotypic analysis revealed that SIMP1 regulates salt tolerance through UMP1A at least in part. Taken together, our work demonstrated that SIMP1 modulates plant salt tolerance by promoting proteasome maturation via UMP1A, therefore mitigating ER stress through enhanced ERAD efficiency under saline conditions.
