Evidence map›Paper›PMID 16244150›Full record

ArticlePlant physiology2005

Arabidopsis FHY1 protein stability is regulated by light via phytochrome A and 26S proteasome.

Yunping Shen, Suhua Feng, Ligeng Ma, Rongcheng Lin, Li-Jia Qu, Zhangliang Chen, Haiyang Wang, Xing Wang Deng

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Plants (Basel, Switzerland) · 2023
    Article
  2. Article
  3. Hinge region ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Article
  5. Photoreceptor partner FHY1 has an independent role in gene modulation and plant development under far-red light.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Phytochrome signaling mechanisms.The arabidopsis book · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. 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

8 authors at 2 institutions in 2 countries.

Yunping ShenPeking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, College of Life Sciences, Peking University, Beijing 100871, China.
Suhua Feng
Ligeng Ma
Rongcheng Lin
Li-Jia Qu
Zhangliang Chen
Haiyang Wang
Xing Wang Deng
National Institute of Biological Sciences, Beijing · CNCornell University · US

Funding

Analysis of a Light-Regulated Development SwitchR37GM047850 · NIGMS · YALE UNIVERSITY · PI DENG, XING WANG · 2004 to 2013
$5.7M
LIGHT SIGNAL TRANDUCTION IN ARABIDOPSISR01GM047850 · NIGMS · YALE UNIVERSITY · PI WEI, NING · 1996 to 2018
$4.1M
LIGHT SIGNAL TRANSDUCTION IN ARABIDOPSISR29GM047850 · NIGMS · YALE UNIVERSITY · PI DENG, XING WANG · 1992 to 1995
–
NIGMS NIH HHS GM47850
6 · The paper itself

Abstract

Phytochrome A (phyA) is the primary photoreceptor mediating responses to far-red light. Among the phyA downstream signaling components, Far-red Elongated Hypocotyl 1 (FHY1) is a genetically defined positive regulator of photomorphogenesis in far-red light. Both physiological and genomic characterization of the fhy1 mutants indicated a close functional relationship of FHY1 with phyA. Here, we showed that FHY1 is most abundant in young seedlings grown in darkness and is quickly down-regulated during further seedling development and by light exposure. By using light-insensitive 35S promoter-driven functional beta-glucuronidase-FHY1 and green fluorescent protein-FHY1 fusion proteins, we showed that this down-regulation of FHY1 protein abundance by light is largely at posttranscriptional level and most evident in the nuclei. The light-triggered FHY1 protein reduction is primarily mediated through the 26S proteasome-dependent protein degradation. Further, phyA is directly involved in mediating the light-triggered down-regulation of FHY1, and the dark accumulation of FHY1 requires functional pleiotropic Constitutive Photomorphogenic/De-Etiolated/Fusca proteins. Our data indicate that phyA, the 26S proteasome, and the Constitutive Photomorphogenic/De-Etiolated/Fusca proteins are all involved in the light regulation of FHY1 protein abundance during Arabidopsis (Arabidopsis thaliana) seedling development.

Indexed as

LightArabidopsisArabidopsis ProteinsCell NucleusCytoplasmDarknessGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantGenes, ReporterHypocotylMutationPhotosynthetic Reaction Center Complex ProteinsPhytochromePhytochrome APlants, Genetically ModifiedProteasome Endopeptidase ComplexArabidopsis ProteinsATP dependent 26S proteaseFHY1 protein, ArabidopsisPhotosynthetic Reaction Center Complex ProteinsPhytochromePhytochrome AProteasome Endopeptidase ComplexRecombinant Fusion Proteins

Identifiers

PMID16244150
PMCPMC1283761
OpenAlexW2049220187

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.