Evidence map›Paper›PMID 41439708›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Dimerization-activated PP2C-D2 and D5 phosphatases negatively regulate brassinosteroid signaling by antagonizing BRI1.

Mengzhan Li, Chunli Liu, Shelley R Hepworth, Yuting Yang, Li Wei, Jim P Fouracre, Suo-Min Wang, Jia Li, Hongju Yin

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Mengzhan LiState Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.ORCID 0000-0001-7170-2323
Chunli LiuState Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.
Shelley R HepworthDepartment of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada.
Yuting YangState Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.
Li WeiState Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.
Jim P FouracreSchool of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdom.ORCID 0000-0003-0049-3047
Suo-Min WangState Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.ORCID 0000-0003-0027-8822
Jia LiGuangdong Provincial Key Laboratory of Plant Adaptation and Molecular Design, Innovation Center for Cell Signal Transduction and Synthetic Biology, School of Life Sciences, Guangzhou University, Guangzhou 510006, China.
Hongju YinState Key Laboratory of Herbage Improvement and Grassland Agro-ecosystems; College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China.ORCID 0000-0002-7235-5420

Funding

China Postdoctoral Science Foundation () 2023M741495Key Technology Research & Development Program of State-owned Assets Supervision and Administration Commission of Gansu Provincial Government 2023GZ008MOST | National Natural Science Foundation of China (NSFC) 32471756
6 · The paper itself

Abstract

Brassinosteroids (BRs) are key hormones that promote plant growth and development. While reversible phosphorylation of the BR receptor BRASSINOSTEROID-INSENSITIVE 1 (BRI1) is critical for BR signaling, much remains to be learned about the dephosphorylation mechanisms of BRI1. Here, we demonstrate that the D-clade type 2C protein phosphatases (PP2C-Ds) negatively regulate BR signaling by dephosphorylating key residues in the kinase activation loop of BRI1. The phosphatase activity of PP2C-D2 and D5 is activated through homo- or heterodimerization, a process antagonized by BR-induced BRI1 phosphorylation or SMALL AUXIN UP RNA15 (SAUR15) binding. BL treatment, BRI1-mediated phosphorylation, or SAUR15 binding disrupts dimerization, returning PPC2C-Ds to a monomeric, inactive state. These data not only reveal another phosphorylation/dephosphorylation cascade regulating BR signaling but also decode unrecognized regulatory mechanisms of PP2C-Ds in plants.

Indexed as

ArabidopsisArabidopsis ProteinsBrassinosteroidsPhosphoprotein PhosphatasesProtein KinasesProtein Phosphatase 2CSignal TransductionGene Expression Regulation, PlantPhosphorylationProtein MultimerizationArabidopsis ProteinsBrassinosteroidsBRI1 protein, ArabidopsisPhosphoprotein PhosphatasesProtein KinasesProtein Phosphatase 2CBRI1dimerizationphosphorylationPP2C-DsSAUR15

Identifiers

PMID41439708
PMCPMC12772178

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.