Evidence map›Paper›PMID 21330376›Full record

ArticleThe Journal of biological chemistry2011

Phosphorylation by CK2 enhances the rapid light-induced degradation of phytochrome interacting factor 1 in Arabidopsis.

Qingyun Bu, Ling Zhu, Michael D Dennis, Lu Yu, Sheen X Lu, Maria D Person, Elaine M Tobin, Karen S Browning, Enamul Huq

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
10.7field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Post-Translational Modifications of TOE3 Regulate Antiviral Defense in Tobacco.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. SlCPK27 cross-links SlHY5 and SlPIF4 in brassinosteroid-dependent photo- and thermo-morphogenesis in tomato.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Phytochrome Signaling Networks.Annual review of plant biology · 2021
    Review
  17. Article
  18. Article
  19. Article
  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

9 authors at 3 institutions in 2 countries.

Qingyun BuSection of Molecular Cell and Developmental Biology, Department of Chemistry and Biochemistry, The Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Ling Zhu
Michael D Dennis
Lu Yu
Sheen X Lu
Maria D Person
Elaine M Tobin
Karen S Browning
Enamul Huq
Institute of Molecular and Cell Biology · RUThe University of Texas at Austin · USUniversity of California, Los Angeles · US

Funding

Pilot Project ProgramP30ES007784 · NIEHS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI RICHIE, ELLEN R · 1996 to 2011
$16.4M
Understanding the basis of circadian rhythms in the model system ArabidopsisR01GM023167 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TOBIN, ELAINE MUNSEY · 1985 to 2010
$4.0M
NIEHS NIH HHS P30 ES007784NIEHS NIH HHS P30ES007784NIGMS NIH HHS GM-23167NIGMS NIH HHS R01 GM023167
6 · The paper itself

Abstract

The phytochrome family of sensory photoreceptors interacts with phytochrome interacting factors (PIFs), repressors of photomorphogenesis, in response to environmental light signals and induces rapid phosphorylation and degradation of PIFs to promote photomorphogenesis. However, the kinase that phosphorylates PIFs is still unknown. Here we show that CK2 directly phosphorylates PIF1 at multiple sites. α1 and α2 subunits individually phosphorylated PIF1 weakly in vitro. However, each of four β subunits strongly stimulated phosphorylation of PIF1 by α1 or α2. Mapping of the phosphorylation sites identified seven Ser/Thr residues scattered throughout PIF1. Ser/Thr to Ala scanning mutations at all seven sites eliminated CK2-mediated phosphorylation of PIF1 in vitro. Moreover, the rate of degradation of the Ser/Thr to Ala mutant PIF1 was significantly reduced compared with wild-type PIF1 in transgenic plants. In addition, hypocotyl lengths of the mutant PIF1 transgenic plants were much longer than the wild-type PIF1 transgenic plants under light, suggesting that the mutant PIF1 is suppressing photomorphogenesis. Taken together, these data suggest that CK2-mediated phosphorylation enhances the light-induced degradation of PIF1 to promote photomorphogenesis.

Indexed as

LightArabidopsisArabidopsis ProteinsBlotting, WesternCasein Kinase IIGene Expression Regulation, PlantIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationPlant ProteinsPlants, Genetically ModifiedArabidopsis ProteinsCasein Kinase IIIntracellular Signaling Peptides and ProteinsPhosphoproteinsPKS1 protein, plantPlant Proteins

Identifiers

PMID21330376
PMCPMC3069410
OpenAlexW2163615702

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.