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保卫细胞脱落酸信号传导中基于氧化还原的蛋白质过硫化作用

Redox-based protein persulfidation in guard cell ABA signaling.

作者信息

Zhou Heng, Zhang Jing, Shen Jie, Zhou Mingjian, Yuan Xingxing, Xie Yanjie

机构信息

Laboratory Center of Life Sciences, College of Life Sciences, Nanjing Agricultural University, Nanjing, PR China.

Institute of Industrial Crops, Jiangsu Academy of Agricultural Sciences, Nanjing, China.

出版信息

Plant Signal Behav. 2020 May 3;15(5):1741987. doi: 10.1080/15592324.2020.1741987. Epub 2020 Mar 17.

Abstract

Hydrogen sulfide (HS) is a versatile signaling molecule that regulates multiple physiological processes in plants, including growth and development, immunity, and stress response as well. Signaling triggered by HS is proposed to occur via persulfidation, an oxidative post-translational modification (PTM) of cysteine residues (-SH) to persulfides (-SSH). Notwithstanding the growing body of information for the plant persulfidation proteome, the gap between the molecular mechanism of HS and physiological functions of protein persulfidation remains large. In this mini-review, we discussed the specific regulatory mechanism of persulfidation on guard cell abscisic acid (ABA) signaling and the possible link of persulfidation, sulfenylation, and S-nitrosylation within the framework of redox-based regulation.

摘要

硫化氢(HS)是一种多功能信号分子,可调节植物中的多种生理过程,包括生长发育、免疫以及应激反应。有人提出,HS引发的信号传导是通过过硫化作用发生的,过硫化作用是半胱氨酸残基(-SH)氧化后翻译修饰(PTM)为过硫化物(-SSH)。尽管有关植物过硫化蛋白质组的信息越来越多,但HS的分子机制与蛋白质过硫化的生理功能之间的差距仍然很大。在这篇小型综述中,我们讨论了过硫化作用对保卫细胞脱落酸(ABA)信号传导的具体调节机制,以及在基于氧化还原的调节框架内过硫化作用、亚磺酰化作用和S-亚硝基化作用之间可能的联系。

相似文献

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Redox-based protein persulfidation in guard cell ABA signaling.保卫细胞脱落酸信号传导中基于氧化还原的蛋白质过硫化作用
Plant Signal Behav. 2020 May 3;15(5):1741987. doi: 10.1080/15592324.2020.1741987. Epub 2020 Mar 17.
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SnRK2.6 phosphorylation/persulfidation: where ABA and HS signaling meet.SnRK2.6 的磷酸化/亚磺化:ABA 和 HS 信号相遇的地方。
Trends Plant Sci. 2021 Dec;26(12):1207-1209. doi: 10.1016/j.tplants.2021.08.005. Epub 2021 Sep 4.

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Mining for protein S-sulfenylation in uncovers redox-sensitive sites.在蛋白质 S-亚磺化修饰组学中挖掘出了氧化还原敏感位点。
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