The cyclic nucleotide cGMP is involved in plant hormone signalling and alters phosphorylation of Arabidopsis thaliana root proteins.

The cyclic nucleotide cGMP is involved in plant hormone signalling and alters phosphorylation of Arabidopsis thaliana root proteins.
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DOI:
10.1093/jxb/ers045
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发表时间:
2012-05
影响因子:
6.9
通讯作者:
Maathuis FJ
Maathuis FJ
中科院分区:
生物学1区
文献类型:
--
作者:
Isner JC;Nühse T;Maathuis FJ

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环核苷酸cGMP在植物的生长发育和对生物和非生物胁迫的响应中起着重要的作用。然而,关于第二信使的确切作用仍然存在许多争议。解开cGMP功能在植物中的进展是阻碍了费力和耗时的方法来测量细胞[cGMP]的变化,但基于荧光的报告的发展已经消除了这个缺点。本研究使用FlincG cGMP报告基因研究植物激素和cGMP信号之间的潜在相互作用,并发现激素脱落酸(阿坝),生长素(IAA)和茉莉酸(JA)对细胞质cGMP水平的快速和显着的影响。相反,油菜素类固醇和细胞分裂素没有引起cGMP信号。阿坝,IAA和JA的影响是明显的外部浓度在纳摩尔范围内的EC 50值约为1000,300和0.03纳摩尔ABA,IAA和JA分别。为了检查酶诱导的cGMP信号如何传播的潜在机制,测试了蛋白磷酸化的作用。拟南芥根微粒体蛋白的磷酸化蛋白质组学分析的情况下,存在和不存在膜渗透性cGMP显示15种蛋白质,迅速(在几分钟内)改变磷酸化状态。其中,9个先前被证明也改变磷酸化状态,以响应植物激素,指出蛋白质磷酸化作为靶点的甜菜碱诱导的cGMP信号传导。
The cyclic nucleotide cGMP has been shown to play important roles in plant development and responses to abiotic and biotic stress. Yet much controversy remains regarding the exact role of this second messenger. Progress in unravelling cGMP function in plants was hampered by laborious and time-consuming methodology to measure changes in cellular [cGMP] but the development of fluorescence-based reporters has removed this disadvantage. This study used the FlincG cGMP reporter to investigate potential interactions between phytohormone and cGMP signalling and found a rapid and significant effect of the hormones abscisic acid (ABA), auxin (IAA), and jasmonic acid (JA) on cytoplasmic cGMP levels. In contrast, brassinosteroids and cytokinin did not evoke a cGMP signal. The effects of ABA, IAA, and JA were apparent at external concentrations in the nanomolar range with EC50 values of around 1000, 300, and 0.03 nmoles for ABA, IAA, and JA respectively. To examine potential mechanisms for how hormone-induced cGMP signals are propagated, the role of protein phosphorylation was tested. A phosphoproteomics analysis on Arabidopsis thaliana root microsomal proteins in the absence and presence of membrane-permeable cGMP showed 15 proteins that rapidly (within minutes) changed in phosphorylation status. Out of these, nine were previously shown to also alter phosphorylation status in response to plant hormones, pointing to protein phosphorylation as a target for hormone-induced cGMP signalling.
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