Evidence map›Paper›PMID 15741320›Full record

ArticleGenes & development2005

HFR1 is targeted by COP1 E3 ligase for post-translational proteolysis during phytochrome A signaling.

In-Cheol Jang, Jun-Yi Yang, Hak Soo Seo, Nam-Hai Chua

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
–field-weighted citation impact
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

150 citing papers in PubMed, 295 citations in OpenAlex.

  1. Article
  2. Review
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  15. Review
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  17. Article
  18. Plant direct · 2022
    Article
  19. International journal of molecular sciences · 2022
    Article
  20. Article

90 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

4 authors at 1 institution in 1 country.

In-Cheol JangLaboratory of Plant Molecular Biology, Rockefeller University, New York, New York 10021, USA.
Jun-Yi Yang
Hak Soo Seo
Nam-Hai Chua
Rockefeller University · US

Funding

LIGHT-RESPONSIVE GENESR01GM044640 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHUA, NAM-HAI · 1991 to 2011
$5.3M
Light Responsive GenesR56GM044640 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHUA, NAM-HAI · 2007 to 2007
$542k
NIGMS NIH HHS GM44640NIGMS NIH HHS R01 GM044640NIGMS NIH HHS R56 GM044640
6 · The paper itself

Abstract

Upon activation by far-red light, phytochrome A signals are transduced through several pathways to promote photomorphogenesis. The COP1 E3 ligase represses photomorphogenesis in part by targeting transcription activators such as LAF1 and HY5 for destruction. Another positive regulator of photomorphogenesis is HFR1, a basic helix-loop-helix (bHLH) transcription factor. Here, we show that HFR1 colocalizes with COP1 in nuclear bodies, and that the HFR1 N-terminal region (amino acids 1-131) interacts with the COP1 WD40 domain. HFR1(DeltaN), an HFR1 mutant lacking the two N-terminal, COP1-interacting motifs, still localizes in nuclear bodies and retains weak affinity for COP1. Both HFR1 and HFR1(DeltaN) can be ubiquitinated by COP1, although with different efficiencies. Expression of 35S-HFR1(DeltaN) in wild-type plants confers greater hypersensitivity to FR than 35S-HFR1 expression, and only seedlings expressing 35S-HFR1(DeltaN) display constitutive photomorphogenesis. These phenotypic differences can be attributed to the instability of HFR1 compared with HFR1(DeltaN). In transgenic plants, HFR1 levels are significantly elevated upon induced expression of a dominant-negative COP1 mutant that interferes with endogenous COP1 E3 activity. Moreover, induced expression of wild-type COP1 in transgenic plants accelerates post-translational degradation of HFR1 under FR light. Taken together, our results show that HFR1 is ubiquitinated by COP1 E3 ligase and marked for post-translational degradation during photomorphogenesis.

Indexed as

Active Transport, Cell NucleusAmino Acid MotifsArabidopsisArabidopsis ProteinsCell NucleusDNA-Binding ProteinsGene Expression Regulation, PlantNuclear ProteinsPhytochromePhytochrome AProtein BindingProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesSignal TransductionUbiquitinUbiquitin-Protein LigasesArabidopsis ProteinsAt1g02340 protein, ArabidopsisAT2G32950 protein, ArabidopsisDNA-Binding ProteinsNuclear ProteinsPHYA protein, ArabidopsisPhytochromePhytochrome AProtein Serine-Threonine KinasesUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID15741320
PMCPMC551579
OpenAlexW2163491393

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.