Evidence map›Paper›PMID 36652487›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

SUMO/deSUMOylation of the BRI1 brassinosteroid receptor modulates plant growth responses to temperature.

Maria Naranjo-Arcos, Moumita Srivastava, Florian Deligne, Prakash Kumar Bhagat, Mansi Mansi, Ari Sadanandom, Grégory Vert

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Nitrate-induced NLP1 SUMOylation regulates nitrate signaling and root nodulation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Dimerization-activated PP2C-D2 and D5 phosphatases negatively regulate brassinosteroid signaling by antagonizing BRI1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
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

7 authors at 2 institutions in 2 countries.

Maria Naranjo-ArcosPlant Science Research Laboratory, Unité Mixte de Recherche 5546 Centre National de la Recherche Scientifique/Université Toulouse 3, 31320 Auzeville Tolosane, France.
Moumita SrivastavaDepartment of Biosciences, Durham University, Durham DH1 3LE, United Kingdom.
Florian DelignePlant Science Research Laboratory, Unité Mixte de Recherche 5546 Centre National de la Recherche Scientifique/Université Toulouse 3, 31320 Auzeville Tolosane, France.ORCID 0000-0001-9697-1730
Prakash Kumar BhagatDepartment of Biosciences, Durham University, Durham DH1 3LE, United Kingdom.ORCID 0000-0001-9693-0250
Mansi MansiDepartment of Biosciences, Durham University, Durham DH1 3LE, United Kingdom.
Ari SadanandomDepartment of Biosciences, Durham University, Durham DH1 3LE, United Kingdom.ORCID 0000-0003-0058-9479
Grégory VertPlant Science Research Laboratory, Unité Mixte de Recherche 5546 Centre National de la Recherche Scientifique/Université Toulouse 3, 31320 Auzeville Tolosane, France.
Durham University · GBCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Brassinosteroids (BRs) are a class of steroid molecules perceived at the cell surface that act as plant hormones. The BR receptor BRASSINOSTEROID INSENSITIVE1 (BRI1) offers a model to understand receptor-mediated signaling in plants and the role of post-translational modifications. Here we identify SUMOylation as a new modification targeting BRI1 to regulate its activity. BRI1 is SUMOylated in planta on two lysine residues, and the levels of BRI1 SUMO conjugates are controlled by the Desi3a SUMO protease. Loss of Desi3a leads to hypersensitivity to BRs, indicating that Desi3a acts as a negative regulator of BR signaling. Besides, we demonstrate that BRI1 is deSUMOylated at elevated temperature by Desi3a, leading to increased BRI1 interaction with the negative regulator of BR signaling BIK1 and to enhanced BRI1 endocytosis. Loss of Desi3a or BIK1 results in increased response to temperature elevation, indicating that BRI1 deSUMOylation acts as a safety mechanism necessary to keep temperature responses in check. Altogether, our work establishes BRI1 deSUMOylation as a molecular crosstalk mechanism between temperature and BR signaling, allowing plants to translate environmental inputs into growth response.

Indexed as

ArabidopsisArabidopsis ProteinsBrassinosteroidsPlant Growth RegulatorsProtein KinasesProtein Serine-Threonine KinasesTemperatureArabidopsis ProteinsBIK1 protein, ArabidopsisBrassinosteroidsBRI1 protein, ArabidopsisPlant Growth RegulatorsProtein KinasesProtein Serine-Threonine KinasesArabidopsisbrassinosteroidsBRI1SUMOtemperature

Identifiers

PMID36652487
PMCPMC9942830
OpenAlexW4317358675

What OpenQuestion 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 OpenQuestion graph.