He Zhouqing, Huang Tingting, Ao Kevin, Yan Xiaofang, Huang Yan
College of Life Sciences, Sichuan Agricultural University, Ya'an, China.
Michael Smith Laboratories, University of British Columbia, Vancouver, BC, Canada.
Front Plant Sci. 2017 Oct 10;8:1682. doi: 10.3389/fpls.2017.01682. eCollection 2017.
Ubiquitination-mediated protein degradation plays a crucial role in the turnover of immune proteins through rapid alteration of protein levels. Specifically, the over-accumulation of immune proteins and consequent activation of immune responses in uninfected cells is prevented through degradation. Protein post-translational modifications can influence and affect ubiquitination. There is accumulating evidence that suggests sumoylation, phosphorylation, and acetylation differentially affect the stability of immune-related proteins, so that control over the accumulation or degradation of proteins is fine-tuned. In this paper, we review the function and mechanism of sumoylation, phosphorylation, acetylation, and ubiquitination in plant disease resistance responses, focusing on how ubiquitination reacts with sumoylation, phosphorylation, and acetylation to regulate plant disease resistance signaling pathways. Future research directions are suggested in order to provide ideas for signaling pathway studies, and to advance the implementation of disease resistance proteins in economically important crops.
泛素化介导的蛋白质降解通过快速改变蛋白质水平在免疫蛋白的周转中起关键作用。具体而言，通过降解可防止免疫蛋白在未感染细胞中的过度积累以及由此引发的免疫反应激活。蛋白质翻译后修饰可影响并作用于泛素化。越来越多的证据表明，SUMO化、磷酸化和乙酰化对免疫相关蛋白的稳定性有不同影响，从而对蛋白质的积累或降解进行微调控制。在本文中，我们综述了SUMO化、磷酸化、乙酰化和泛素化在植物抗病反应中的功能和机制，重点关注泛素化如何与SUMO化、磷酸化和乙酰化相互作用以调节植物抗病信号通路。我们还提出了未来的研究方向，以便为信号通路研究提供思路，并推动抗病蛋白在重要经济作物中的应用。
