Quantitative analysis of changes in the phosphoproteome of maize induced by the plant hormone salicylic acid.
Quantitative analysis of changes in the phosphoproteome of maize induced by the plant hormone salicylic acid.
复制标题
植物激素水杨酸诱导玉米磷酸化蛋白质组变化的定量分析
DOI：
10.1038/srep18155
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发表时间：
2015-12-11
影响因子：
4.6
通讯作者：
Chen Y
中科院分区：
文献类型：
--
作者：
Wu L;Hu X;Wang S;Tian L;Pang Y;Han Z;Wu L;Chen Y
植物激素水杨酸（SA）在调节多种生理生化过程中起着重要作用。我们以前的研究确定了几个蛋白激酶响应SA，这表明磷酸化事件在植物响应SA中起着重要作用。在这项研究中，我们的特点是磷酸化蛋白质组的玉米响应SA使用同位素标记的相对和绝对定量（iTRAQ）技术和TiO 2富集法。通过LC-MS/MS分析，在1495个磷酸肽中，我们发现了858个磷酸蛋白。其中，291磷酸肽对应的244磷蛋白被发现后SA处理显着变化。鉴定的磷蛋白参与广泛的生物过程，这表明对SA的反应包括主要细胞过程的重新格式化。此外，一些以前不知道参与SA的磷蛋白被发现有显着改变磷酸化水平。许多这些变化是磷酸化减少，表明其他目前未知的SA信号通路，导致下游靶点的磷酸化减少，必须参与。我们的研究首次尝试在全球磷酸化蛋白质组分析响应SA，并提供了更好地了解SA调节的分子机制。
Phytohormone salicylic acid (SA) plays an important role in regulating various physiological and biochemical processes. Our previous study identified several protein kinases responsive to SA, suggesting that phosphorylation events play an important role in the plant response to SA. In this study, we characterized the phosphoproteome of maize in response to SA using isotope tags for relative and absolute quantification (iTRAQ) technology and TiO2 enrichment method. Based on LC-MS/MS analysis, we found a total of 858 phosphoproteins among 1495 phosphopeptides. Among them, 291 phosphopeptides corresponding to 244 phosphoproteins were found to be significantly changed after SA treatment. The phosphoproteins identified are involved in a wide range of biological processes, which indicate that the response to SA encompasses a reformatting of major cellular processes. Furthermore, some of the phosphoproteins which were not previously known to be involved with SA were found to have significantly changed phosphorylation levels. Many of these changes are phosphorylation decreases, indicating that other currently unknown SA signaling pathways that result in decreased phosphorylation of downstream targets must be involved. Our study represents the first attempt at global phosphoproteome profiling in response to SA and provides a better understanding of the molecular mechanisms regulated by SA.