Publication Information
Wang et al., 2018
Abstract
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 K(1)(2)(3), Yang Z(1)(2)(3)(4), Qing D(1)(2)(3), Ren F(1)(2)(3), Liu
S(1)(2)(3), Zheng Q(1)(2)(3)(5), Liu J(6), Zhang W(6), Dai C(5), Wu M(1)(2)(3),
Chehab EW(7), Braam J(7), Li N(8)(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.
Comment in
Nat Plants. 2018 Nov;4(11):856.
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.
DOI: 10.1073/pnas.1814006115
PMCID: PMC6205429
PMID: 30291188 [Indexed for MEDLINE]
Conflict of interest statement: The authors declare no conflict of interest.
