AMPK activity is required for the induction of anhydrobiosis in a tardigrade Hypsibius exemplaris , and its potential up‐regulator is PP2A
AMPK activity is required for the induction of anhydrobiosis in a tardigrade Hypsibius exemplaris , and its potential up‐regulator is PP2A
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AMPK 活性是缓步动物 Hypsibius exemplaris 中诱导脱水所需的，其潜在的上调因子是 PP2A
DOI：
10.1111/gtc.12726
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发表时间：
2019
期刊：
影响因子：
2.1
通讯作者：
Arakawa Kazuharu
中科院分区：
文献类型：
--
作者：
Kondo Koyuki;Mori Masaru;Tomita Masaru;Arakawa Kazuharu
脱水缓步动物Hypsibius exemplaris以前被认为需要从头基因表达和蛋白磷酸酶1（PP 1）和蛋白磷酸酶2A（PP 2A）活性才能成功脱水。这些结果表明，H. experimental是响应干旱胁迫的信号转导系统，其中磷酸化事件参与其中。为此，我们对轻度干燥胁迫下的红球藻进行了时间序列磷酸化蛋白质组学研究，检测到48种具有显著差异调节的磷酸化蛋白。其中，观察到AMP活化蛋白激酶（AMPK）磷酸化水平的立即和连续降低。随后的化学遗传学方法表明，AMPK在脱水预处理阶段被激活，抑制其活性会损害成功的脱水。由于PP 2A已知在其他生物体中使AMPK去磷酸化，我们认为在轻度干燥胁迫下AMPK磷酸化水平降低是由PP 2A去磷酸化引起的。因此，用PP 1/PP 2A抑制剂甘草酸（CA）预处理的动物的磷酸化蛋白质组学缺乏AMPK磷酸化水平的降低。这些结果表明，AMPK的活性是成功的脱水生活所必需的，其磷酸化状态可能是由PP 2A调节。
The anhydrobiotic tardigrade,Hypsibius exemplaris,was previously considered to require de novo gene expression and protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) activity for successful anhydrobiosis. These indicate thatH. exemplarishas signal transduction systems responding to desiccation stress, with the involvement of phosphorylation events. To this end, we carried out time‐series phosphoproteomicsof H. exemplarisexposed to mild desiccation stress and detected 48 phosphoproteins with significant differential regulations. Among them, immediate and successive reduction of phosphorylation levels of AMP‐activated protein kinase (AMPK) was observed. The subsequent chemical genetic approach showed that AMPK was activated during the preconditioning stage for anhydrobiosis, and inhibition of its activity impaired successful anhydrobiosis. As PP2A is known to dephosphorylate AMPK in other organisms, we suggested that decreased phosphorylation levels of AMPK upon mild desiccation stress were caused by dephosphorylation by PP2A. Accordingly, phosphoproteomics of animals pre‐treated with the PP1/PP2A inhibitor cantharidic acid (CA) lacked the decrease in phosphorylation levels of AMPK. These observations suggest that AMPK activity is required for successful anhydrobiosis inH. exemplaris, and its phosphorylation state is possibly regulated by PP2A.