Evidence map›Paper›PMID 19141709›Full record

ArticleThe Plant cell2009

Formation of nuclear bodies of Arabidopsis CRY2 in response to blue light is associated with its blue light-dependent degradation.

Xuhong Yu, Ricardo Sayegh, Maskit Maymon, Katherine Warpeha, John Klejnot, Hongyun Yang, Jie Huang, Janet Lee, Lon Kaufman, Chentao Lin

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
9.3field-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

86 citing papers in PubMed, 144 citations in OpenAlex.

  1. Review
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  11. Review
  12. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Functions of COP1/SPA E3 Ubiquitin Ligase Mediated by MpCRY in the LiverwortInternational journal of molecular sciences · 2021
    Article
  20. Article

26 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

10 authors at 2 institutions in 1 country.

Xuhong YuDepartment of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, California 90095, USA.
Ricardo Sayegh
Maskit Maymon
Katherine Warpeha
John Klejnot
Hongyun Yang
Jie Huang
Janet Lee
Lon Kaufman
Chentao Lin
University of California, Los Angeles · USUniversity of Illinois Chicago · US

Funding

The signaling mechanisms of Arabidopsis CRY2R01GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 2001 to 2021
$9.5M
PLANT PHOTOSENSORY RECEPTOR CRY2--SIGNALING MECHANISMR29GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 1997 to 2001
$204k
NIGMS NIH HHS GM56265NIGMS NIH HHS R01 GM056265NIGMS NIH HHS R29 GM056265
6 · The paper itself

Abstract

Arabidopsis thaliana cryptochrome 2 (CRY2) mediates photoperiodic promotion of floral initiation and blue light inhibition of hypocotyl elongation. It has been hypothesized that photoexcitation derepresses CRY2 by disengaging its C-terminal domain from the N-terminal PHR domain. To test this hypothesis, we analyzed activities of CRY2 fused to green fluorescent protein (GFP) at either the N terminus (GFP-CRY2) or the C terminus (CRY2-GFP). While GFP-CRY2 exerts light-dependent biochemical and physiological activities similar to those of the endogenous CRY2, CRY2-GFP showed constitutive biochemical and physiological activities. CRY2-GFP is constitutively phosphorylated, it promotes deetiolation in both dark and light, and it activates floral initiation in both long-day and short-day photoperiods. These results are consistent with the hypothesis that photoexcited CRY2 disengages its C-terminal domain from the PHR domain to become active. Surprisingly, we found that CRY2-GFP, but not GFP-CRY2, formed distinct nuclear bodies in response to blue light. Compared with GFP-CRY2 or the endogenous CRY2, CRY2-GFP degradation was significantly retarded in response to blue light, suggesting that the nuclear bodies may result from accumulation of photoexcited CRY2-GFP waiting to be degraded. Consistent with this interpretation, we showed that both GFP-CRY2 and endogenous CRY2 formed nuclear bodies in the presence of the 26S-proteasome inhibitors that block blue light-dependent CRY2 degradation.

Indexed as

LightArabidopsisArabidopsis ProteinsCryptochromesFlavoproteinsGene Expression Regulation, PlantGreen Fluorescent ProteinsIntranuclear Inclusion BodiesModels, MolecularPhosphorylationPhotoreceptors, PlantProteasome Endopeptidase ComplexRecombinant Fusion ProteinsRNA, PlantArabidopsis ProteinsATP dependent 26S proteaseCRY1 protein, ArabidopsisCRY2 protein, ArabidopsisCryptochromesFlavoproteinsGreen Fluorescent ProteinsPhotoreceptors, PlantProteasome Endopeptidase ComplexRecombinant Fusion ProteinsRNA, Plant

Identifiers

PMID19141709
PMCPMC2648085
OpenAlexW2123792065

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.