UBC18 E2 conjugating enzyme depends on SINAT1 E3 ligase to destabilize the ESCRT component FREE1 in plant iron deficiency responses

文献类型： 外文期刊

第一作者： Liu, Chuanliang

作者： Liu, Chuanliang;Zhang, Tianrui;Liu, Weijie;Xiao, Zhidan;Yang, Chao;Peng, Changlian;Gao, Caiji;Shen, Wenjin;Li, Hongbo;Xiao, Zhidan;Xiao, Zhidan;Xiao, Zhidan;Yang, Chao;Yang, Chao

作者机构：

关键词： Arabidopsis; E2 ubiquitin-conjugating enzyme; UBC18; FREE1; stability; iron deficiency

期刊名称：PLANT JOURNAL （ 影响因子：5.7； 五年影响因子：7.0 ）

ISSN： 0960-7412

年卷期： 2024 年 120 卷 5 期

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收录情况： SCI

摘要： E2 ubiquitin-conjugating enzymes play a crucial role in the ubiquitination process by catalyzing ubiquitin transfer. Although the function of ubiquitin-protein ligases (E3s) in plants response to diverse abiotic stress by targeting specific substrates has been well studied, the involvement of E2s in environmental responses and their downstream targets are not well understood. In this study, we demonstrated that the E2 ubiquitin-conjugating enzyme 18 (UBC18) influences the stability of FREE1 to modulate iron deficiency stress. UBC18 affects the ubiquitination of FREE1 and promotes its degradation, and overexpression of UBC18 decreases plants' sensitivity to iron deficiency by reducing FREE1 level, whereas the ubc18 mutant exhibits sensitivity due to elevated FREE1 accumulation. This study also identified that lysine residues K227, K295, K315, and K540 are required for FREE1 ubiquitination and stability regulation. Mutating these lysine residues in FREE1 resulted in plants' sensitivity to iron starvation. Taken together, our findings shed light on the mechanism of UBC18 in responding to iron deficiency stress by modulating the abundance of FREE1, and further elucidate the role of ubiquitination sites in FREE1 stability regulation and the plant iron deficiency response.

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