Evidence map›Paper›PMID 30529286›Full record

ArticleGenomics, proteomics & bioinformatics2018

RNF126 Quenches RNF168 Function in the DNA Damage Response.

Lianzhong Zhang, Zhenzhen Wang, Ruifeng Shi, Xuefei Zhu, Jiahui Zhou, Bin Peng, Xingzhi Xu

Open access · goldAbstract read
In one paragraph

Article in Genomics, proteomics & bioinformatics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Emerging Roles of RNF168 in Tumor Progression.Molecules (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
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

7 authors at 3 institutions in 1 country.

Lianzhong ZhangCollege of Life Sciences, Capital Normal University, Beijing 100048, China; Faculty of Life Sciences, Tangshan Normal College, Tangshan 063000, China.
Zhenzhen WangCollege of Life Sciences, Capital Normal University, Beijing 100048, China.
Ruifeng ShiCollege of Life Sciences, Capital Normal University, Beijing 100048, China; Guangdong Key Laboratory for Genome Stability & Disease Prevention, Shenzhen University Health Science Center, Shenzhen 518060, China.
Xuefei ZhuGuangdong Key Laboratory for Genome Stability & Disease Prevention, Shenzhen University Health Science Center, Shenzhen 518060, China.
Jiahui ZhouCollege of Life Sciences, Capital Normal University, Beijing 100048, China.
Bin PengGuangdong Key Laboratory for Genome Stability & Disease Prevention, Shenzhen University Health Science Center, Shenzhen 518060, China.
Xingzhi XuCollege of Life Sciences, Capital Normal University, Beijing 100048, China; Guangdong Key Laboratory for Genome Stability & Disease Prevention, Shenzhen University Health Science Center, Shenzhen 518060, China. Electronic address: Xingzhi.Xu@szu.edu.cn.
Shenzhen University Health Science Center · CNCapital Normal University · CNTangshan Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA damage response (DDR) is essential for maintaining genome stability and protecting cells from tumorigenesis. Ubiquitin and ubiquitin-like modifications play an important role in DDR, from signaling DNA damage to mediating DNA repair. In this report, we found that the E3 ligase ring finger protein 126 (RNF126) was recruited to UV laser micro-irradiation-induced stripes in a RNF8-dependent manner. RNF126 directly interacted with and ubiquitinated another E3 ligase, RNF168. Overexpression of wild type RNF126, but not catalytically-inactive mutant RNF126 (CC229/232AA), diminished ubiquitination of H2A histone family member X (H2AX), and subsequent bleomycin-induced focus formation of total ubiquitin FK2, TP53-binding protein 1 (53BP1), and receptor-associated protein 80 (RAP80). Interestingly, both RNF126 overexpression and RNF126 downregulation compromised homologous recombination (HR)-mediated repair of DNA double-strand breaks (DSBs). Taken together, our findings demonstrate that RNF126 negatively regulates RNF168 function in DDR and its appropriate cellular expression levels are essential for HR-mediated DSB repair.

Indexed as

DNA Breaks, Double-StrandedCarrier ProteinsCell Line, TumorDNA-Binding ProteinsDNA RepairGenomic InstabilityHeLa CellsHistone ChaperonesHistonesHumansNuclear ProteinsRNA InterferenceRNA, Small InterferingSignal TransductionTumor Suppressor p53-Binding Protein 1UbiquitinCarrier ProteinsDNA-Binding ProteinsHistone ChaperonesHistonesNuclear ProteinsRNA, Small InterferingRNF126 protein, humanRNF168 protein, humanRNF8 protein, humanTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1UbiquitinUbiquitin-Protein LigasesUIMC1 protein, humanDNA damage responseDNA repairRNF126RNF168RNF8Ubiquitination

Identifiers

PMID30529286
PMCPMC6411902
OpenAlexW2902339720

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.