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酪氨酰蛋白硫酸转移酶通过对 SnRK2.2/2.3/2.6 的硫酸化来抑制 ABA 信号通路。

Tyrosylprotein sulfotransferase suppresses ABA signaling via sulfation of SnRK2.2/2.3/2.6.

机构信息

State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Taian, 271018, China.

Department of Food Science and Engineering, Shandong Agriculture and Engineering University, Jinan, 250100, China.

出版信息

J Integr Plant Biol. 2023 Aug;65(8):1846-1851. doi: 10.1111/jipb.13493. Epub 2023 May 16.

DOI:10.1111/jipb.13493
PMID:37052306
Abstract

Phytohormone abscisic acid (ABA) plays vital roles in stress tolerance, while long-term overactivation of ABA signaling suppresses plant growth and development. However, the braking mechanism of ABA responses is not clear. Protein tyrosine sulfation catalyzed by tyrosylprotein sulfotransferase (TPST) is a critical post-translational modification. Through genetic screening, we identified a tpst mutant in Arabidopsis that was hypersensitive to ABA. In-depth analysis revealed that TPST could interact with and sulfate SnRK2.2/2.3/2.6, which accelerated their degradation and weakened the ABA signaling. Taken together, these findings uncovered a novel mechanism of desensitizing ABA responses via protein sulfation.

摘要

植物激素脱落酸(ABA)在胁迫耐受中发挥着重要作用,而 ABA 信号的长期过度激活会抑制植物的生长和发育。然而,ABA 响应的制动机制尚不清楚。由酪氨酸蛋白硫酸转移酶(TPST)催化的蛋白酪氨酸硫酸化是一种关键的翻译后修饰。通过遗传筛选,我们在拟南芥中鉴定到一个对 ABA 超敏感的 tpst 突变体。深入分析表明,TPST 可以与 SnRK2.2/2.3/2.6 相互作用并使其硫酸化,从而加速它们的降解并减弱 ABA 信号。综上所述,这些发现揭示了通过蛋白硫酸化来脱敏 ABA 响应的新机制。

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