Quantitative and functional posttranslational modification proteomics reveals that TREPH1 plays a role in plant touch-delayed bolting
Quantitative and functional posttranslational modification proteomics reveals that TREPH1 plays a role in plant touch-delayed bolting
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定量和功能翻译后修饰蛋白质组学揭示 TREPH1 在植物接触延迟抽苔中发挥作用
DOI:
10.1073/pnas.1814006115
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发表时间:
2018-08
影响因子:
11.1
通讯作者:
Li Ning
中科院分区:
文献类型:
--
作者:
Wang Kai;Yang Zhu;Qing Dongjin;Ren Feng;Liu Shichang;Zheng Qingsong;Liu Jun;Zhang Weiping;Dai Chen;Wu Madeline;Chehab E Wassim;Braam Janet;Li Ning
Significance Plants respond to a delicate force signal, such as a light touch, similar to animal neural systems, as demonstrated by thigmotropism, thigmonastic movement, and thigmomorphogenesis. To understand the force-signaling networks, we applied stable isotope labeling in Arabidopsis (SILIA)-based quantitative posttranslational modification proteomics to assess protein phosphorylation changes in Arabidopsis subjected to 40-second cotton-swab touch, identified 4,895 nonredundant phosphopeptides, 579 of which are previously unreported phosphosites derived from 509 phosphoprotein groups, and identified 24 TOUCH-REGULATED PHOSPHOPROTEIN (TREPH) groups. Molecular biological, genetic, and bioinformatic analyses revealed that the previously uncharacterized TREPH1 protein is required for the bolting-delay aspect of the Arabidopsis touch response. These studies suggest that protein phosphorylation and the TREPH1 protein are critical for the mechanotransduction pathway leading to an aspect of plant thigmomorphogenesis. Environmental mechanical forces, such as wind and touch, trigger gene-expression regulation and developmental changes, called “thigmomorphogenesis,” in plants, demonstrating the ability of plants to perceive such stimuli. In Arabidopsis, a major thigmomorphogenetic response is delayed bolting, i.e., emergence of the flowering stem. The signaling components responsible for mechanotransduction of the touch response are largely unknown. Here, we performed a high-throughput SILIA (stable isotope labeling in Arabidopsis)-based quantitative phosphoproteomics analysis to profile changes in protein phosphorylation resulting from 40 seconds of force stimulation in Arabidopsis thaliana. Of the 24 touch-responsive phosphopeptides identified, many were derived from kinases, phosphatases, cytoskeleton proteins, membrane proteins, and ion transporters. In addition, the previously uncharacterized protein TOUCH-REGULATED PHOSPHOPROTEIN1 (TREPH1) became rapidly phosphorylated in touch-stimulated plants, as confirmed by immunoblots. TREPH1 fractionates as a soluble protein and is shown to be required for the touch-induced delay of bolting and gene-expression changes. Furthermore, a nonphosphorylatable site-specific isoform of TREPH1 (S625A) failed to restore touch-induced flowering delay of treph1-1, indicating the necessity of S625 for TREPH1 function and providing evidence consistent with the possible functional relevance of the touch-regulated TREPH1 phosphorylation. Taken together, these findings identify a phosphoprotein player in Arabidopsis thigmomorphogenesis regulation and provide evidence that TREPH1 and its touch-induced phosphorylation may play a role in touch-induced bolting delay, a major component of thigmomorphogenesis.
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影响因子:
5.6
作者:
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通讯作者:
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