Wurzinger Bernhard, Mair Andrea, Fischer-Schrader Katrin, Nukarinen Ella, Roustan Valentin, Weckwerth Wolfram, Teige Markus
Department of Ecogenomics and Systems Biology, University of Vienna, Austria.
Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, Germany.
FEBS Lett. 2017 Nov;591(21):3625-3636. doi: 10.1002/1873-3468.12852. Epub 2017 Oct 4.
The evolutionarily highly conserved SNF1-related protein kinase (SnRK1) protein kinase is a metabolic master regulator in plants, balancing the critical energy consumption between growth- and stress response-related metabolic pathways. While the regulation of the mammalian [AMP-activated protein kinase (AMPK)] and yeast (SNF1) orthologues of SnRK1 is well-characterised, the regulation of SnRK1 kinase activity in plants is still an open question. Here we report that the activity and T-loop phosphorylation of AKIN10, the kinase subunit of the SnRK1 complex, is regulated by the redox status. Although this regulation is dependent on a conserved cysteine residue, the underlying mechanism is different to the redox regulation of animal AMPK and has functional implications for the regulation of the kinase complex in plants under stress conditions.
进化上高度保守的SNF1相关蛋白激酶（SnRK1）是植物中的一种代谢主调节器，平衡生长和应激反应相关代谢途径之间的关键能量消耗。虽然SnRK1在哺乳动物中的直系同源物[AMP激活的蛋白激酶（AMPK）]和酵母中的直系同源物（SNF1）的调节已得到充分表征，但植物中SnRK1激酶活性的调节仍是一个悬而未决的问题。在这里，我们报告SnRK1复合体的激酶亚基AKIN10的活性和T环磷酸化受氧化还原状态调节。尽管这种调节依赖于一个保守的半胱氨酸残基，但其潜在机制与动物AMPK的氧化还原调节不同，并且对胁迫条件下植物中激酶复合体的调节具有功能意义。
