Evidence map›Paper›PMID 27091446›Full record

ArticleThe Journal of cell biology2016

ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair.

Ekaterina Gracheva, Shalaka Chitale, Thomas Wilhelm, Alexander Rapp, Jonathan Byrne, Jens Stadler, Rebeca Medina, M Cristina Cardoso, Holger Richly

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  7. Epigenetic Regulation of Nucleotide Excision Repair.Frontiers in cell and developmental biology · 2022
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Ekaterina GrachevaLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany.
Shalaka ChitaleLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany.
Thomas WilhelmLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany.
Alexander RappDepartment of Biology, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Jonathan ByrneLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany.
Jens StadlerLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany.
Rebeca MedinaLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany.
M Cristina CardosoDepartment of Biology, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Holger RichlyLaboratory of Molecular Epigenetics, Institute of Molecular Biology, 55128 Mainz, Germany h.richly@imb-mainz.de.
Institute of Molecular Biology · DETechnical University of Darmstadt · DE

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
NIH HHS P40 OD010440
6 · The paper itself

Abstract

Faithful DNA repair is essential to maintain genome integrity. Ultraviolet (UV) irradiation elicits both the recruitment of DNA repair factors and the deposition of histone marks such as monoubiquitylation of histone H2A at lesion sites. Here, we report how a ubiquitin E3 ligase complex specific to DNA repair is remodeled at lesion sites in the global genome nucleotide excision repair (GG-NER) pathway. Monoubiquitylation of histone H2A (H2A-ubiquitin) is catalyzed predominantly by a novel E3 ligase complex consisting of DDB2, DDB1, CUL4B, and RING1B (UV-RING1B complex) that acts early during lesion recognition. The H2A-ubiquitin binding protein ZRF1 mediates remodeling of this E3 ligase complex directly at the DNA lesion site, causing the assembly of the UV-DDB-CUL4A E3 ligase complex (DDB1-DDB2-CUL4A-RBX1). ZRF1 is an essential factor in GG-NER, and its function at damaged chromatin sites is linked to damage recognition factor XPC. Overall, the results shed light on the interplay between epigenetic and DNA repair recognition factors at DNA lesion sites.

Indexed as

Cullin ProteinsDNA-Binding ProteinsDNA DamageDNA RepairHEK293 CellsHistonesHumansMolecular ChaperonesOncogene ProteinsPolycomb Repressive Complex 1RNA-Binding ProteinsUbiquitinationUbiquitin-Protein LigasesUltraviolet RaysCUL4B protein, humanCullin ProteinsDDB1 protein, humanDDB2 protein, humanDNA-Binding ProteinsDNAJC2 protein, humanHistonesMolecular ChaperonesOncogene ProteinsPolycomb Repressive Complex 1RNA-Binding ProteinsRNF2 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID27091446
PMCPMC5084270
OpenAlexW2340991188

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.