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Proc Natl Acad Sci U S A. 2018 Oct 23;115(43):E10265-E10274. doi: 10.1073/pnas.1814006115. Epub 2018 Oct 5.

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

Wang K1,2,3, Yang Z1,2,3,4, Qing D1,2,3, Ren F1,2,3, Liu S1,2,3, Zheng Q1,2,3,5, Liu J6, Zhang W6, Dai C5, Wu M1,2,3, Chehab EW7, Braam J7, Li N8,2,3,4.

Author information

1
Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, China.
2
Energy Institute, The Hong Kong University of Science and Technology, Hong Kong SAR, China.
3
Institute for the Environment, The Hong Kong University of Science and Technology, Hong Kong SAR, China.
4
HKUST Shenzhen Research Institute, 518057 Shenzhen, China.
5
Proteomics Center, College of Resources and Environmental Sciences, Nanjing Agricultural University, 210095 Nanjing, China.
6
ASPEC Technologies Limited, 100101 Beijing, China.
7
Department of BioSciences, Rice University, Houston, TX 77005.
8
Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, China; boningli@ust.hk.

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 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.

KEYWORDS:

4C PTM proteomics; TREPH1; force-induced phosphoproteome; thigmomorphogenesis; touch-regulated phosphoprotein

Comment in

PMID:
30291188
PMCID:
PMC6205429
DOI:
10.1073/pnas.1814006115
[Indexed for MEDLINE]
Free PMC Article

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