Medicago falcata MfSTMIR, an E3 ligase of endoplasmic reticulum-associated degradation, is involved in salt stress response

文献类型： 外文期刊

第一作者： Zhang, Rongxue

作者： Zhang, Rongxue;Chen, Hong;Duan, Mei;Zhu, Fugui;Dong, Jiangli;Wang, Tao;Zhang, Rongxue;Wen, Jiangqi

作者机构：

关键词： endoplasmic reticulum-associated degradation; unfolded protein response; endoplasmic reticulum stress; salt stress; Medicago

期刊名称：PLANT JOURNAL （ 影响因子：6.417； 五年影响因子：7.627 ）

ISSN： 0960-7412

年卷期： 2019 年 98 卷 4 期

页码：

收录情况： SCI

摘要： Recent studies on E3 of endoplasmic reticulum (ER)-associated degradation (ERAD) in plants have revealed homologs in yeast and animals. However, it remains unknown whether the plant ERAD system contains a plant-specific E3 ligase. Here, we report that MfSTMIR, which encodes an ER-membrane-localized RING E3 ligase that is highly conserved in leguminous plants, plays essential roles in the response of ER and salt stress in Medicago. MfSTMIR expression was induced by salt and tunicamycin (Tm). mtstmir loss-of-function mutants displayed impaired induction of the ER stress-responsive genes BiP1/2 and BiP3 under Tm treatment and sensitivity to salt stress. MfSTMIR promoted the degradation of a known ERAD substrate, CPY*. MfSTMIR interacted with the ERAD-associated ubiquitin-conjugating enzyme MtUBC32 and Sec61-translocon subunit MtSec61 gamma. MfSTMIR did not affect MtSec61 gamma protein stability. Our results suggest that the plant-specific E3 ligase MfSTMIR participates in the ERAD pathway by interacting with MtUBC32 and MtSec61 gamma to relieve ER stress during salt stress.

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