Evidence map›Paper›PMID 26994443›Full record

ArticleDNA repair2016

The role of HERC2 and RNF8 ubiquitin E3 ligases in the promotion of translesion DNA synthesis in the chicken DT40 cell line.

Mohiuddin, Shunsuke Kobayashi, Islam Shamima Keka, Guillaume Guilbaud, Julian Sale, Takeo Narita, H Ismail Abdel-Aziz, Xin Wang, Saki Ogawa, Hiroyuki Sasanuma and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in DNA repair, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

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  11. SUMOylation of PCNA by PIAS1 and PIAS4 promotes template switch in the chicken and human B cell lines.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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

14 authors at 6 institutions in 5 countries.

MohiuddinDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan.
Shunsuke KobayashiDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan.
Islam Shamima KekaDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan.
Guillaume GuilbaudMedical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Julian SaleMedical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Takeo NaritaDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan; Department of Proteomics, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark.
H Ismail Abdel-AzizDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan; Faculty of Medicine, Seuz Canal University, circular road Ez-Eldeen, Ismailia 41522, Egypt.
Xin WangDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan.
Saki OgawaDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan.
Hiroyuki SasanumaDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan.
Roland ChiuUniversity College Groningen, University of Groningen, 9718 BG Groningen, Hoendiepskade 23-24, The Netherlands.
Vibe H OestergaardDepartment of Biology, University of Copenhagen, DK-2200 Copenhagen N, Denmark.
Michael LisbyDepartment of Biology, University of Copenhagen, DK-2200 Copenhagen N, Denmark.
Shunichi TakedaDepartment of Radiation Genetics, Kyoto University Graduate School of Medicine, Yoshida Konoe, Sakyo-ku, Kyoto 606-8501, Japan. Electronic address: stakeda@rg.med.kyoto-u.ac.jp.
Kyoto University · JPUniversity of Copenhagen · DKMedical Research Council · GBMRC Laboratory of Molecular Biology · GBNovo Nordisk Foundation · DKUniversity of Groningen · NL

Funding

Medical Research Council MC_U105178808Worldwide Cancer Research 05-0160Worldwide Cancer Research 08-0017Worldwide Cancer Research 11-0514
6 · The paper itself

Abstract

The replicative DNA polymerases are generally blocked by template DNA damage. The resulting replication arrest can be released by one of two post-replication repair (PRR) pathways, translesion DNA synthesis (TLS) and template switching by homologous recombination (HR). The HERC2 ubiquitin ligase plays a role in homologous recombination by facilitating the assembly of the Ubc13 ubiquitin-conjugating enzyme with the RNF8 ubiquitin ligase. To explore the role of HERC2 and RNF8 in PRR, we examined immunoglobulin diversification in chicken DT40 cells deficient in HERC2 and RNF8. Unexpectedly, the HERC2(-/-) and RNF8(-/-) cells and HERC2(-/-)/RNF8(-/-) double mutant cells exhibit a significant reduction in the rate of immunoglobulin (Ig) hypermutation, compared to wild-type cells. Further, the HERC2(-/-) and RNF8(-/-) mutants exhibit defective maintenance of replication fork progression immediately after exposure to UV while retaining proficient post-replicative gap filling. These mutants are both proficient in mono-ubiquitination of PCNA. Taken together, these results suggest that HERC2 and RNF8 promote TLS past abasic sites and UV-lesions at or very close to stalled replication forks.

Indexed as

DNA ReplicationAnimalsChickensDNA DamageGuanine Nucleotide Exchange FactorsHEK293 CellsHumansMutationUbiquitinationUbiquitin-Protein LigasesUltraviolet RaysGuanine Nucleotide Exchange FactorsUbiquitin-Protein LigasesHERC2Post-replication repairRNF8Translesion DNA synthesisUbiquitination

Identifiers

PMID26994443
PMCPMC5351851
OpenAlexW2290010311

What OpenQuestion holds

Textmetadata
LicenceTDM
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.