Abstract
Plants are exposed to diverse mechanical forces, such as gravity, touch, and wind, which significantly impact their growth, development, and adaptation to the environment. While plant mechanoresponse are known to be temporally regulated, the underlying cellular and molecular mechanisms remain incompletely characterized. In Arabidopsis, prolonged mechanical stimulation induces thigmomorphogenesis responses characterized by shorter inflorescence stems, delayed flowering, and reduced rosette size. A previous phosphoproteomics study identified Touch-Regulated Phosphoprotein 1 (TREPH1) as a key early-response component, showing rapid phosphorylation within 40 seconds of stimulation and mediating touch-induced transcriptomic changes. To investigate the underlying mechanisms systematically, we developed an optimized biotinylproteomics workflow incorporating proximity labeling technology and dimethyl labeling-based quantitative proteomics.With in-depth biotinylproteomics, a proximal protein network centered on TREPH1 was constructed with 49 SPBs, and highlighted the role of the plastid division protein FtsZ1 in plant mechanoresponse. Furthermore, this strategy was extended to characterize the nuclear pore complex proxiome, profiling 19 known Arabidopsis nucleoporins and 59 non-nucleoporins as potential regulators in the nucleus mechanotransduction events. The integrated analysis provided unprecedented insights into the dynamic protein networks governing thigmomorphogenesis, advancing understanding of plant mechanosensing and response systems from molecule level to organelle coordinated mechanoresponse in the model organism Arabidopsis. The developed methodologies here also provide templates for studying dynamic protein networks and profiling stable protein complexes in plant mechanobiology.
| Date of Award | 2025 |
|---|---|
| Original language | English |
| Awarding Institution |
|
| Supervisor | Pingbo HUANG (Supervisor) |
Cite this
- Standard