Evidence map›Paper›PMID 10990463›Full record

ArticleThe EMBO journal2000

HY5 stability and activity in arabidopsis is regulated by phosphorylation in its COP1 binding domain.

C S Hardtke, K Gohda, M T Osterlund, T Oyama, K Okada, X W Deng

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed
24.3field-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

153 citing papers in PubMed, 384 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Post-Translational Modifications of TOE3 Regulate Antiviral Defense in Tobacco.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  6. Disruption ofPlants (Basel, Switzerland) · 2025
    Article
  7. Review
  8. Review
  9. Ubiquitin-specific protease UBP14 stabilizes HY5 by deubiquitination to promote photomorphogenesis inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Light signaling as cellular integrator of multiple environmental cues in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  15. Review
  16. CRISPR/Cas9-MediatedInternational journal of molecular sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Article

93 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

C S HardtkeDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8104, USA.
K Gohda
M T Osterlund
T Oyama
K Okada
X W Deng
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis HY5 is a bZIP transcription factor that promotes photomorphogenesis. Previous studies suggested that COP1, a negative regulator of photomorphogenesis, directly interacts with nuclear HY5 and targets it for proteasome-mediated degradation. Light negatively regulates the nuclear level of COP1 and thus permits HY5 accumulation. Here we report that HY5 abundance peaks in early seedling development, consistent with its role in promoting photomorphogenesis. HY5 acts exclusively within a complex and exists in two isoforms, resulting from phosphorylation within its COP1 binding domain by a light- regulated kinase activity. Unphosphorylated HY5 shows stronger interaction with COP1, is the preferred substrate for degradation, has higher affinity to target promoters and is physiologically more active than the phosphorylated version. Therefore, HY5 phosphorylation provides an added level of light-mediated regulation of HY5 stability and activity besides nuclear COP1 levels. Regulated HY5 phosphorylation not only provides abundant and physiologically more active unphosphorylated HY5 in the light, but also helps to maintain a small pool of less active phosphorylated HY5 in the dark, which could be essential for a rapid initial response during dark-to-light transition.

Indexed as

Arabidopsis ProteinsUbiquitin-Protein LigasesAmino Acid SequenceArabidopsisBasic-Leucine Zipper Transcription FactorsBinding SitesBlotting, WesternCarrier ProteinsCasein Kinase IICell NucleusChromatography, GelGlutathione TransferaseLightMolecular Sequence DataNuclear ProteinsPhosphorylationArabidopsis ProteinsAT2G32950 protein, ArabidopsisBasic-Leucine Zipper Transcription FactorsCarrier ProteinsCasein Kinase IIGlutathione TransferaseHY5 protein, ArabidopsisNuclear ProteinsPlant ProteinsProtein IsoformsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID10990463
PMCPMC314229
OpenAlexW2014770852

What OpenQuestion holds

Textmetadata
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.