The U-box ubiquitin ligase TUD1 promotes brassinosteroid-induced GSK2 degradation in rice.

The U-box ubiquitin ligase TUD1 promotes brassinosteroid-induced GSK2 degradation in rice.
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U-box泛素连接酶TUD1促进油菜素类固醇诱导的水稻GSK2降解

DOI:
10.1016/j.xplc.2022.100450
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发表时间:
2023-03-13
影响因子:
10.5
通讯作者:
Tong, Hongning
Tong, Hongning
中科院分区:
生物学1区
文献类型:
--
作者:
Liu, Dapu;Zhang, Xiaoxing;Li, Qingliang;Xiao, Yunhua;Zhang, Guoxia;Yin, Wenchao;Niu, Mei;Meng, Wenjing;Dong, Nana;Liu, Jihong;Yang, Yanzhao;Xie, Qi;Chu, Chengcai;Tong, Hongning

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油菜素内酯(BRs)是一类在作物改良中具有巨大潜力的类固醇激素。去抑制通常是激素信号传导的关键事件之一。然而,水稻(Oryza sativa) BR信号的中心负调控因子GSK2的稳定性是如何被BR调控的仍然是未知的。本研究通过酵母双杂交筛选,确定U-box泛素连接酶TUD1为gsk2相互作用蛋白。我们发现TUD1能够直接与GSK2相互作用并使其泛素化。tud1突变体的表型与具有组成型激活GSK2的植物的表型高度相似。与这一发现一致,与野生型相比,GSK2蛋白在tud1突变体中积累。此外,抑制BR合成可促进GSK2积累,抑制TUD1的稳定性。相反,BRs可以诱导GSK2降解,但促进TUD1积累。此外,在tud1中,GSK2的降解过程在很大程度上受到BR的影响。总之,我们的研究证明了TUD1在BR诱导的GSK2降解中的作用,从而促进了我们对水稻BR信号通路关键步骤的理解。U-box泛素连接酶TUD1与油菜素内酯信号抑制剂GSK2相互作用,并通过26S蛋白酶体促进GSK2泛素化和降解。tud1突变体和gsk2激活的植株在植株结构、籽粒形态、分子和细胞变化方面高度相似。br诱导的GSK2降解需要TUD1,油菜素内酯促进TUD1的积累。
Brassinosteroids (BRs) are a class of steroid hormones with great potential for use in crop improvement. De-repression is usually one of the key events in hormone signaling. However, how the stability of GSK2, the central negative regulator of BR signaling in rice (Oryza sativa), is regulated by BRs remains elusive. Here, we identify the U-box ubiquitin ligase TUD1 as a GSK2-interacting protein by yeast two-hybrid screening. We show that TUD1 is able to directly interact with GSK2 and ubiquitinate the protein. Phenotypes of the tud1 mutant are highly similar to those of plants with constitutively activated GSK2. Consistent with this finding, GSK2 protein accumulates in the tud1 mutant compared with the wild type. In addition, inhibition of BR synthesis promotes GSK2 accumulation and suppresses TUD1 stability. By contrast, BRs can induce GSK2 degradation but promote TUD1 accumulation. Furthermore, the GSK2 degradation process is largely impaired in tud1 in response to BR. In conclusion, our study demonstrates the role of TUD1 in BR-induced GSK2 degradation, thereby advancing our understanding of a critical step in the BR signaling pathway of rice. The U-box ubiquitin ligase TUD1 interacts with the brassinosteroid signal inhibitor GSK2 and promotes GSK2 ubiquitination and degradation via the 26S proteasome. The tud1 mutant and GSK2-activated plants are highly similar in terms of plant architecture, grain morphology, and molecular and cellular changes. TUD1 is required for BR-induced GSK2 degradation, and brassinosteroids promote TUD1 accumulation.
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