Evidence map›Paper›PMID 30598506›Full record

ArticleThe Journal of biological chemistry2019

Ribosomal protein L6 (RPL6) is recruited to DNA damage sites in a poly(ADP-ribose) polymerase-dependent manner and regulates the DNA damage response.

Chuanzhen Yang, Weicheng Zang, Yapeng Ji, Tingting Li, Yongfeng Yang, Xiaofeng Zheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 60 citations in OpenAlex.

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  15. Comparative Transcriptomic Analysis of Three Common Liver Cell Lines.International journal of molecular sciences · 2023
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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

6 authors at 1 institution in 1 country.

Chuanzhen YangFrom the State Key Lab of Protein and Plant Gene Research and.
Weicheng ZangFrom the State Key Lab of Protein and Plant Gene Research and.
Yapeng JiFrom the State Key Lab of Protein and Plant Gene Research and.
Tingting LiFrom the State Key Lab of Protein and Plant Gene Research and.
Yongfeng YangFrom the State Key Lab of Protein and Plant Gene Research and.
Xiaofeng ZhengFrom the State Key Lab of Protein and Plant Gene Research and xiaofengz@pku.edu.cn.ORCID 0000-0001-6790-0669
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomal proteins are the building blocks of ribosome biogenesis. Beyond their known participation in ribosome assembly, the ribosome-independent functions of ribosomal proteins are largely unknown. Here, using immunoprecipitation, subcellular fractionation, His-ubiquitin pulldown, and immunofluorescence microscopy assays, along with siRNA-based knockdown approaches, we demonstrate that ribosomal protein L6 (RPL6) directly interacts with histone H2A and is involved in the DNA damage response (DDR). We found that in response to DNA damage, RPL6 is recruited to DNA damage sites in a poly(ADP-ribose) polymerase (PARP)-dependent manner, promoting its interaction with H2A. We also observed that RPL6 depletion attenuates the interaction between mediator of DNA damage checkpoint 1 (MDC1) and H2A histone family member X, phosphorylated (γH2AX), impairs the accumulation of MDC1 at DNA damage sites, and reduces both the recruitment of ring finger protein 168 (RNF168) and H2A Lys-15 ubiquitination (H2AK15ub). These RPL6 depletion-induced events subsequently inhibited the recruitment of the following downstream repair proteins: tumor protein P53-binding protein 1 (TP53BP1) and BRCA1, DNA repair-associated (BRCA1). Moreover, the RPL6 knockdown resulted in defects in the DNA damage-induced G

Indexed as

DNA DamageDNA RepairBRCA1 ProteinCell CycleCell SurvivalHEK293 CellsHeLa CellsHistonesHumansPoly (ADP-Ribose) Polymerase-1Ribosomal ProteinsSignal TransductionUbiquitinUbiquitinationBRCA1 ProteinBRCA1 protein, humanHistonesPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1ribosomal protein L6Ribosomal ProteinsUbiquitincell signalingDNA damage responseDNA repairE3 ubiquitin ligasehistonehistone H2AMDC1PARPRibosomal Protein L6ubiquitylation (ubiquitination)

Identifiers

PMID30598506
PMCPMC6393625
OpenAlexW2907518674

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.