Evidence map›Paper›PMID 29042542›Full record

ArticleNature communications2017

Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation.

Keiichirou Nemoto, Abdelaziz Ramadan, Gen-Ichiro Arimura, Kenichiro Imai, Kentaro Tomii, Kazuo Shinozaki, Tatsuya Sawasaki

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
9.6field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Review
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  6. Genome-Wide Investigation ofInternational journal of molecular sciences · 2025
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Emerging Functions of Protein Tyrosine Phosphatases in Plants.International journal of molecular sciences · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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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 5 institutions in 2 countries.

Keiichirou NemotoProteo-Science Center (PROS), Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime, 790-8577, Japan.
Abdelaziz RamadanProteo-Science Center (PROS), Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime, 790-8577, Japan.
Gen-Ichiro ArimuraFaculty of Industrial Science & Technology, Department of Biological Science & Technology, Tokyo University of Science, Tokyo, 125-8585, Japan.
Kenichiro ImaiArtificial Intelligence Research Center (AIRC) and Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), 2-4-7 Aomi, Koto Ward, Tokyo, 135-0064, Japan.
Kentaro TomiiArtificial Intelligence Research Center (AIRC) and Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), 2-4-7 Aomi, Koto Ward, Tokyo, 135-0064, Japan.ORCID http://orcid.org/0000-0002-4567-4768
Kazuo ShinozakiGene Discovery Research Group, RIKEN Center for Sustainable Resource Science, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.
Tatsuya SawasakiProteo-Science Center (PROS), Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime, 790-8577, Japan. sawasaki@ehime-u.ac.jp.
Ehime University · JPNational Institute of Advanced Industrial Science and Technology · JPAin Shams University · EGRIKEN Center for Sustainable Resource Science · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gibberellin (GA) is a major hormone for plant growth and development. GA response is derived from the degradation of DELLA repressor proteins after GA-dependent complex formation of the GID1 GA receptor with DELLA. Genistein is a known tyrosine (Tyr) kinase inhibitor and inhibits DELLA degradation. However, the biological role of Tyr phosphorylation on the GA response remains unclear. Here, we demonstrate that GARU (GA receptor RING E3 ubiquitin ligase) mediates ubiquitin-dependent degradation of GID1, and that the TAGK2 plant Tyr-kinase is a target of genistein and inhibits GARU-GID1A interactions by phosphorylation of GARU at Tyr321. Genistein induces degradation of GID1 and accumulation of DELLA. Conversely, Arabidopsis garu mutant and TAGK2-overexpressing plants accelerate GID1 stabilization and DELLA degradation. Under salt stress, GARU suppresses seed germination. We propose that GA response is negatively regulated by GARU-dependent GID1 ubiquitination and positively by Tyr phosphorylation of GARU by TAGK2, and genistein inhibits GA signaling by TAGK2 inhibition.Plants respond to gibberellins via GID1-dependent degradation of DELLA proteins. Here, Nemoto et al. show that the gibberellin response is positively regulated by tyrosine phosphorylation of GARU, an E3 ubiquitin ligase that mediates degradation of GID1.

Indexed as

ArabidopsisArabidopsis ProteinsGenisteinGibberellinsPhosphorylationPlants, Genetically ModifiedProtein Serine-Threonine KinasesReceptors, Cell SurfaceSalinitySeedsTranscription FactorsUbiquitinationUbiquitin-Protein LigasesArabidopsis ProteinsERF13 protein, ArabidopsisGARU protein, ArabidopsisGenisteingibberellic acidGibberellinsGID1a protein, ArabidopsisProtein Serine-Threonine KinasesReceptors, Cell SurfaceTAGK2 protein, ArabidopsisTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID29042542
PMCPMC5645313
OpenAlexW2763528155

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.