Evidence map›Paper›PMID 27325768›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

BBX21, an Arabidopsis B-box protein, directly activates HY5 and is targeted by COP1 for 26S proteasome-mediated degradation.

Dongqing Xu, Yan Jiang, Jigang Li, Fang Lin, Magnus Holm, Xing Wang Deng

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed, 1 pooled it
41.8field-weighted citation impact, top 1% 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

125 citing papers in PubMed, 1 synthesis or guideline pooled it, 284 citations in OpenAlex.

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  20. Elucidating the Role ofInternational journal of molecular sciences · 2024
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65 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

6 authors at 4 institutions in 2 countries.

Dongqing XuState Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Center for Life Sciences, School of Advanced Agriculture Sciences and School of Life Sciences, Peking University, Beijing 100871, China;
Yan JiangState Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Center for Life Sciences, School of Advanced Agriculture Sciences and School of Life Sciences, Peking University, Beijing 100871, China;
Jigang LiState Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China;
Fang LinState Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Center for Life Sciences, School of Advanced Agriculture Sciences and School of Life Sciences, Peking University, Beijing 100871, China;
Magnus HolmDepartment of Biological and Environmental Sciences, Gothenburg University, SE-405 30 Gothenburg, Sweden.
Xing Wang DengState Key Laboratory of Protein and Plant Gene Research, Peking-Tsinghua Center for Life Sciences, School of Advanced Agriculture Sciences and School of Life Sciences, Peking University, Beijing 100871, China; deng@pku.edu.cn.
Center for Life Sciences · CNPeking University · CNChina Agricultural University · CNUniversity of Gothenburg · SE

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
NIGMS NIH HHS R01 GM047850NIGMS NIH HHS R37 GM047850
6 · The paper itself

Abstract

BBX21 (also known as SALT TOLERANCE HOMOLOG 2), a B-box (BBX)-containing protein, has been previously identified as a positive regulator of light signaling; however, the precise role of BBX21 in regulating seedling photomorphogenesis remains largely unclear. In this study, we report that CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) interacts with BBX21 in vivo and is able to ubiquitinate BBX21 in vitro. Thus, BBX21 is targeted for 26S proteasome-mediated degradation in dark-grown Arabidopsis seedlings in a COP1-dependent manner. Moreover, we show that BBX21 binds to the T/G-box in the ELONGATED HYPOCOTYL 5 (HY5) promoter and directly activates HY5 expression in the light. Transgenic seedlings overexpressing BBX21 exhibit dramatically shortened hypocotyls in the light, and this phenotype is dependent on a functional HY5. Taken together, our data suggest a molecular base underlying BBX21-mediated seedling photomorphogenesis, indicating that BBX21 is a pivotal component involved in the COP1-HY5 regulatory hub.

Indexed as

ArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsGene ExpressionGene Expression Regulation, PlantLightNuclear ProteinsPlants, Genetically ModifiedProteasome Endopeptidase ComplexTranscription FactorsUbiquitinationUbiquitin-Protein LigasesArabidopsis ProteinsAT2G32950 protein, ArabidopsisATP dependent 26S proteaseBasic-Leucine Zipper Transcription FactorsBBX21 protein, ArabidopsisHY5 protein, ArabidopsisNuclear ProteinsProteasome Endopeptidase ComplexTranscription FactorsUbiquitin-Protein LigasesArabidopsisBBX21COP1HY5photomorphogenesis

Identifiers

PMID27325768
PMCPMC4941485
OpenAlexW2469025158

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.