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Dimerization-activated PP2C-D2 and D5 phosphatases negatively regulate brassinosteroid signaling by antagonizing
Mengzhan Li1,2, Chunli Liu1, Shelley R Hepworth3
1State Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.
D-clade type 2C protein phosphatases (PP2C-Ds) regulate plant growth by dephosphorylating the brassinosteroid (BR) receptor BRI1. Their activity is controlled by dimerization, which is disrupted by BR signaling, revealing a new regulatory mechanism.
Area of Science:
- Plant biology
- Molecular signaling
- Biochemistry
Background:
- Brassinosteroids (BRs) are crucial plant hormones regulating growth and development.
- The BR receptor BRASSINOSTEROID-INSENSITIVE 1 (BRI1) is activated by phosphorylation, but its dephosphorylation remains poorly understood.
Purpose of the Study:
- To investigate the role of D-clade type 2C protein phosphatases (PP2C-Ds) in regulating BR signaling.
- To elucidate the dephosphorylation mechanisms of the BRI1 receptor.
Main Methods:
- Investigated the interaction between PP2C-Ds and BRI1.
- Assessed the phosphatase activity of PP2C-D2 and PP2C-D5.
- Analyzed the effect of BR treatment, BRI1 phosphorylation, and SAUR15 binding on PP2C-D dimerization and activity.
Main Results:
- PP2C-Ds negatively regulate BR signaling by dephosphorylating BRI1's kinase activation loop.
- PP2C-D phosphatase activity is activated by homo- or heterodimerization.
- BR treatment, BRI1 phosphorylation, or SAUR15 binding disrupts PP2C-D dimerization, leading to inactivation.
Conclusions:
- Identified PP2C-Ds as key negative regulators of BR signaling through BRI1 dephosphorylation.
- Revealed a novel phosphorylation/dephosphorylation cascade controlling BR signaling.
- Uncovered that PP2C-D dimerization is a critical regulatory mechanism for their activity in plants.
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