Evidence map›Paper›PMID 30104204›Full record

ArticleEMBO reports2018

DNA damage-induced replication stress results in PA200-proteasome-mediated degradation of acetylated histones.

Imke K Mandemaker, Marit E Geijer, Iris Kik, Karel Bezstarosti, Erikjan Rijkers, Anja Raams, Roel C Janssens, Hannes Lans, Jan Hj Hoeijmakers, Jeroen Aa Demmers and 2 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 50 citations in OpenAlex.

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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

12 authors at 1 institution in 2 countries.

Imke K MandemakerDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.
Marit E GeijerDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.ORCID 0000-0001-9453-6997
Iris KikDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.
Karel BezstarostiProteomics Center, Erasmus University Medical Center, Rotterdam, The Netherlands.
Erikjan RijkersProteomics Center, Erasmus University Medical Center, Rotterdam, The Netherlands.
Anja RaamsDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.
Roel C JanssensDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.
Hannes LansDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.ORCID 0000-0003-4417-5358
Jan Hj HoeijmakersDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.
Jeroen Aa DemmersProteomics Center, Erasmus University Medical Center, Rotterdam, The Netherlands.
Wim VermeulenDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.
Jurgen A MarteijnDepartment of Molecular Genetics, Oncode Institute, Erasmus University Medical Center, Rotterdam, The Netherlands J.Marteijn@erasmusmc.nl.ORCID 0000-0001-9321-518X
Erasmus MC · NL

Funding

European Research Council 340988
6 · The paper itself

Abstract

Histone acetylation influences protein interactions and chromatin accessibility and plays an important role in the regulation of transcription, replication, and DNA repair. Conversely, DNA damage affects these crucial cellular processes and induces changes in histone acetylation. However, a comprehensive overview of the effects of DNA damage on the histone acetylation landscape is currently lacking. To quantify changes in histone acetylation, we developed an unbiased quantitative mass spectrometry analysis on affinity-purified acetylated histone peptides, generated by differential parallel proteolysis. We identify a large number of histone acetylation sites and observe an overall reduction of acetylated histone residues in response to DNA damage, indicative of a histone-wide loss of acetyl modifications. This decrease is mainly caused by DNA damage-induced replication stress coupled to specific proteasome-dependent loss of acetylated histones. Strikingly, this degradation of acetylated histones is independent of ubiquitylation but requires the PA200-proteasome activator, a complex that specifically targets acetylated histones for degradation. The uncovered replication stress-induced degradation of acetylated histones represents an important chromatin-modifying response to cope with replication stress.

Indexed as

AcetylationAmino Acid SequenceChromatinDNA DamageDNA RepairDNA ReplicationHistonesHumansNuclear ProteinsProteasome Endopeptidase ComplexProteolysisUbiquitinationChromatinHistonesNuclear ProteinsProteasome Endopeptidase ComplexPSME4 protein, humanacetylationDNA damagehistonePA200‐proteasomereplication stress

Identifiers

PMID30104204
PMCPMC6172457
OpenAlexW2885935989

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.