期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 115, 期 43, 页码 E10265-E10274出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1814006115
关键词
thigmomorphogenesis; force-induced phosphoproteome; 4C PTM proteomics; touch-regulated phosphoprotein; TREPH1
资金
- National Science Foundation of China [31370315, 31570187]
- Research Grants Council of Hong Kong [661613, 16101114, 16103615, 16103817, AoE/M-403/16]
- Energy Institute of HKUST [SRF11EG17PG-A, SRFI11EG17-A]
- Croucher Foundation Chinese Academy of Science-HKUST Joint Laboratory Matching Fund [SBI09/10.EG01-A]
- Rice 04 Sponsorship Scheme for Targeted Strategic Partnerships
- Guangdong-Hong Kong Key Area Breakthrough Program Grant [GDST16SC02]
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 (5625A) failed to restore touchinduced flowering delay of trephl-1, indicating the necessity of 5625 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.
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