Evidence map›Paper›PMID 18552200›Full record

ArticleThe Plant cell2008

Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin ligase with DDB1 and CUL4 that is involved in multiple plant developmental processes.

Yu Zhang, Suhua Feng, Fangfang Chen, Haodong Chen, Jia Wang, Chad McCall, Yue Xiong, Xing Wang Deng

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
4.3field-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

84 citing papers in PubMed, 165 citations in OpenAlex.

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  19. A single helix repression domain is functional across diverse eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2022
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24 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

8 authors at 3 institutions in 2 countries.

Yu ZhangPeking-Yale Joint Center of Plant Molecular Genetics and Agrobiotechnology, College of Life Sciences, Peking University, Beijing 100871, China.
Suhua Feng
Fangfang Chen
Haodong Chen
Jia Wang
Chad McCall
Yue Xiong
Xing Wang Deng
National Institute of Biological Sciences, Beijing · CNUNC Lineberger Comprehensive Cancer CenterYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human DDB1-CUL4 ASSOCIATED FACTOR (DCAF) proteins have been reported to interact directly with UV-DAMAGED DNA BINDING PROTEIN1 (DDB1) through the WDxR motif in their WD40 domain and function as substrate-recognition receptors for CULLIN4-based E3 ubiquitin ligases. Here, we identified and characterized a homolog of human DCAF1/VprBP in Arabidopsis thaliana. Yeast two-hybrid analysis demonstrated the physical interaction between DCAF1 and DDB1 from Arabidopsis, which is likely mediated via the WD40 domain of DCAF1 that contains two WDxR motifs. Moreover, coimmunoprecipitation assays showed that DCAF1 associates with DDB1, RELATED TO UBIQUITIN-modified CUL4, and the COP9 signalosome in vivo but not with CULLIN-ASSOCIATED and NEDDYLATION-DISSOCIATED1, CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1), or the COP10-DET1-DDB1 complex, supporting the existence of a distinct Arabidopsis CUL4 E3 ubiquitin ligase, the CUL4-DDB1-DCAF1 complex. Transient expression of fluorescently tagged DCAF1, DDB1, and CUL4 in onion epidermal cells showed their colocalization in the nucleus, consistent with the notion that the CUL4-DDB1-DCAF1 complex functions as a nuclear E3 ubiquitin ligase. Genetic and phenotypic analysis of two T-DNA insertion mutants of DCAF1 showed that embryonic development of the dcaf1 homozygote is arrested at the globular stage, indicating that DCAF1 is essential for plant embryogenesis. Reducing the levels of DCAF1 leads to diverse developmental defects, implying that DCAF1 might be involved in multiple developmental pathways.

Indexed as

Amino Acid MotifsAmino Acid SequenceArabidopsisArabidopsis ProteinsCullin ProteinsDNA, BacterialDNA-Binding ProteinsGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantHumansImmunoprecipitationIntracellular Signaling Peptides and ProteinsMolecular Sequence DataMutagenesis, InsertionalNuclear ProteinsOnionsArabidopsis ProteinsAT2G32950 protein, ArabidopsisCOP10 protein, ArabidopsisCULLIN4 protein, ArabidopsisCullin ProteinsDET1 protein, ArabidopsisDNA, BacterialDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsT-DNAUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID18552200
PMCPMC2483375
OpenAlexW2123781861

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.