Quantitative and functional posttranslational modification proteomics reveals that TREPH1 plays a role in plant touch-delayed bolting

Kai Wang, Zhu YANG, Dongjin Qing, Feng Ren, Shichang Liu, Qingsong Zheng, Jun Liu, Weiping Zhang, Chen Dai, Madeline Wu, E. Wassim Chehab, Janet Braam, Ning Li*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

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 touchresponsive 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 touchinduced 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 touchinduced phosphorylation may play a role in touch-induced bolting delay, a major component of thigmomorphogenesis.

Original languageEnglish
Pages (from-to)E10265-E10274
JournalProceedings of the National Academy of Sciences of the United States of America
Volume115
Issue number43
DOIs
Publication statusPublished - 23 Oct 2018

Scopus Subject Areas

  • General

User-Defined Keywords

  • 4C PTM proteomics
  • Force-induced phosphoproteome
  • Thigmomorphogenesis
  • Touch-regulated phosphoprotein
  • TREPH1

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