Evidence map›Paper›PMID 22732244›Full record

ArticlePlant physiology2012

The light-response BTB1 and BTB2 proteins assemble nuclear ubiquitin ligases that modify phytochrome B and D signaling in Arabidopsis.

Matthew J Christians, Derek J Gingerich, Zhihua Hua, Timothy D Lauer, Richard D Vierstra

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. CUL3Science advances · 2026
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  17. Differing biophysical properties underpin the unique signaling potentials within the plant phytochrome photoreceptor families.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

5 authors at 2 institutions in 1 country.

Matthew J ChristiansDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706, USA.
Derek J Gingerich
Zhihua Hua
Timothy D Lauer
Richard D Vierstra
University of Wisconsin–Eau Claire · USUniversity of Wisconsin–Madison · US

Funding

Analysis of ASKs, Components of SCF Ubiquitin-LigasesF32GM068361 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI GINGERICH, DEREK J · 2003 to 2005
$139k
NIGMS NIH HHS GM68361
6 · The paper itself

Abstract

Members of the Bric-a-Brac/Tramtrack/Broad Complex (BTB) family direct the selective ubiquitylation of proteins following their assembly into Cullin3-based ubiquitin ligases. Here, we describe a subfamily of nucleus-localized BTB proteins encoded by the LIGHT-RESPONSE BTB1 (LRB1) and LRB2 loci in Arabidopsis (Arabidopsis thaliana) that strongly influences photomorphogenesis. Whereas single lrb1 and lrb2 mutants are relatively normal phenotypically, double mutants are markedly hypersensitive to red light, but not to far-red or blue light, and are compromised in multiple photomorphogenic processes, including seed germination, cotyledon opening and expansion, chlorophyll accumulation, shade avoidance, and flowering time. This red light hypersensitivity can be overcome by eliminating phytochrome B (phyB) and phyD, indicating that LRB1/2 act downstream of these two photoreceptor isoforms. Levels of phyB/D proteins but not their messenger RNAs are abnormally high in light-grown lrb1 lrb2 plants, implying that their light-dependent turnover is substantially dampened. Whereas other red light-hypersensitive mutants accumulate phyA protein similar to or higher than the wild type in light, the lrb1 lrb2 mutants accumulate less, suggesting that LRB1/2 also positively regulate phyA levels in a phyB/D-dependent manner. Together, these data show that the BTB ubiquitin ligases assembled with LRB1/2 function redundantly as negative regulators of photomorphogenesis, possibly by influencing the turnover of phyB/D.

Indexed as

LightSignal TransductionApoproteinsArabidopsisArabidopsis ProteinsCell NucleusColorCotyledonEpistasis, GeneticFlowersGene Expression Regulation, PlantGenetic LociGerminationNuclear ProteinsPhytochromePhytochrome BApoproteinsArabidopsis ProteinsLRB1 protein, ArabidopsisLRB2 protein, ArabidopsisLRB3 protein, ArabidopsisNuclear ProteinsPHYB protein, ArabidopsisPHYD protein, ArabidopsisPhytochromePhytochrome BUbiquitin-Protein Ligases

Identifiers

PMID22732244
PMCPMC3440189
OpenAlexW2149829053

What OpenQuestion holds

Textmetadata
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.