Evidence map›Paper›PMID 30615605›Full record

ArticlePLoS genetics2019

BRASSINOSTEROID-SIGNALING KINASE 3, a plasma membrane-associated scaffold protein involved in early brassinosteroid signaling.

Hong Ren, Björn C Willige, Yvon Jaillais, Sa Geng, Mee Yeon Park, William M Gray, Joanne Chory

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
24.1field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 119 citations in OpenAlex.

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  7. OsBSK3 and OsBSK2 regulate grain size and leaf angle via MAPK signaling pathway in rice.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
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  10. Frontiers in plant science · 2025
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  11. Review
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  13. Review
  14. Article
  15. Article
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  17. Article
  18. Arabidopsis proteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. 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

7 authors at 3 institutions in 2 countries.

Hong RenHoward Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, California, United States of America.ORCID 0000-0002-8402-0468
Björn C WilligePlant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California, United States of America.
Yvon JaillaisPlant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California, United States of America.
Sa GengPlant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California, United States of America.
Mee Yeon ParkDepartment of Plant and Microbial Biology, University of Minnesota, Saint Paul, Minnesota, United States of America.
William M GrayDepartment of Plant and Microbial Biology, University of Minnesota, Saint Paul, Minnesota, United States of America.ORCID 0000-0002-1320-290X
Joanne ChoryHoward Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, California, United States of America.
Salk Institute for Biological Studies · USUniversity of Minnesota · USUniversité Claude Bernard Lyon 1 · FR

Funding

Molecular mechanisms of auxin response in ArabidopsisR01GM067203 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI GRAY, WILLIAM M · 2003 to 2020
$3.5M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM067203
6 · The paper itself

Abstract

Brassinosteroids (BRs) are steroid hormones essential for plant growth and development. The BR signaling pathway has been studied in some detail, however, the functions of the BRASSINOSTEROID-SIGNALING KINASE (BSK) family proteins in the pathway have remained elusive. Through forward genetics, we identified five semi-dominant mutations in the BSK3 gene causing BSK3 loss-of-function and decreased BR responses. We therefore investigated the function of BSK3, a receptor-like cytoplasmic kinase, in BR signaling and plant growth and development. We find that BSK3 is anchored to the plasma membrane via N-myristoylation, which is required for its function in BR signaling. The N-terminal kinase domain is crucial for BSK3 function, and the C-terminal three tandem TPR motifs contribute to BSK3/BSK3 homodimer and BSK3/BSK1 heterodimer formation. Interestingly, the effects of BSK3 on BR responses are dose-dependent, depending on its protein levels. Our genetic studies indicate that kinase dead BSK3K86R protein partially rescues the bsk3-1 mutant phenotypes. BSK3 directly interacts with the BSK family proteins (BSK3 and BSK1), BRI1 receptor kinase, BSU1 phosphatase, and BIN2 kinase. BIN2 phosphorylation of BSK3 enhances BSK3/BSK3 homodimer and BSK3/BSK1 heterodimer formation, BSK3/BRI1 interaction, and BSK3/BSU1 interaction. Furthermore, we find that BSK3 upregulates BSU1 transcript and protein levels to activate BR signaling. BSK3 is broadly expressed and plays an important role in BR-mediated root growth, shoot growth, and organ separation. Together, our findings suggest that BSK3 may function as a scaffold protein to regulate BR signaling. The results of our studies provide new insights into early BR signaling mechanisms.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBrassinosteroidsGene Expression Regulation, PlantLoss of Function MutationPhenotypePhosphoprotein PhosphatasesPhosphorylationPlants, Genetically ModifiedProtein Serine-Threonine KinasesSignal TransductionArabidopsis ProteinsBrassinosteroidsbrassinosteroid-signaling kinase3, ArabidopsisBSU1 protein, ArabidopsisPhosphoprotein PhosphatasesProtein Serine-Threonine Kinases

Identifiers

PMID30615605
PMCPMC6336344
OpenAlexW2907933728

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.