Evidence map›Paper›PMID 24939902›Full record

ArticleNucleic acids research2014

CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis.

Ornella Cazzalini, Sabrina Sommatis, Micol Tillhon, Ilaria Dutto, Angela Bachi, Alexander Rapp, Tiziana Nardo, A Ivana Scovassi, Daniela Necchi, M Cristina Cardoso and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 105 citations in OpenAlex.

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  13. Molecular insight into the PCNA-binding mode of FBH1.Structure (London, England : 1993) · 2023
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  18. Revisiting the Function of p21International journal of molecular sciences · 2022
    Review
  19. Review
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1 more citing papers are in PubMed but not listed here.

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 4 institutions in 2 countries.

Ornella CazzaliniDepartment of Molecular Medicine, University of Pavia, Pavia 27100, Italy.
Sabrina SommatisDepartment of Molecular Medicine, University of Pavia, Pavia 27100, Italy.
Micol TillhonInstitute of Molecular Genetics, National Research Council (CNR), Pavia 27100, Italy.
Ilaria DuttoInstitute of Molecular Genetics, National Research Council (CNR), Pavia 27100, Italy.
Angela BachiIFOM-FIRC Institute of Molecular Oncology, Milan 20100, Italy.
Alexander RappTechnische Universität Darmstadt, Darmstadt 64287, Germany.
Tiziana NardoInstitute of Molecular Genetics, National Research Council (CNR), Pavia 27100, Italy.
A Ivana ScovassiInstitute of Molecular Genetics, National Research Council (CNR), Pavia 27100, Italy.
Daniela NecchiDepartment of Drug Sciences, University of Pavia, Pavia 27100, Italy.
M Cristina CardosoTechnische Universität Darmstadt, Darmstadt 64287, Germany.
Lucia A StivalaDepartment of Molecular Medicine, University of Pavia, Pavia 27100, Italy.
Ennio ProsperiInstitute of Molecular Genetics, National Research Council (CNR), Pavia 27100, Italy prosperi@igm.cnr.it.
National Research Council · ITUniversity of Pavia · ITTechnical University of Darmstadt · DEFIRC Institute of Molecular Oncology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proliferating cell nuclear antigen (PCNA) protein serves as a molecular platform recruiting and coordinating the activity of factors involved in multiple deoxyribonucleic acid (DNA) transactions. To avoid dangerous genome instability, it is necessary to prevent excessive retention of PCNA on chromatin. Although PCNA functions during DNA replication appear to be regulated by different post-translational modifications, the mechanism regulating PCNA removal and degradation after nucleotide excision repair (NER) is unknown. Here we report that CREB-binding protein (CBP), and less efficiently p300, acetylated PCNA at lysine (Lys) residues Lys13,14,77 and 80, to promote removal of chromatin-bound PCNA and its degradation during NER. Mutation of these residues resulted in impaired DNA replication and repair, enhanced the sensitivity to ultraviolet radiation, and prevented proteolytic degradation of PCNA after DNA damage. Depletion of both CBP and p300, or failure to load PCNA on DNA in NER deficient cells, prevented PCNA acetylation and degradation, while proteasome inhibition resulted in accumulation of acetylated PCNA. These results define a CBP and p300-dependent mechanism for PCNA acetylation after DNA damage, linking DNA repair synthesis with removal of chromatin-bound PCNA and its degradation, to ensure genome stability.

Indexed as

DNA RepairAcetylationCells, CulturedChromatinCREB-Binding ProteinDNADNA DamageDNA-Directed DNA PolymeraseDNA ReplicationHumansMutationp300-CBP-Associated Factorp300-CBP Transcription FactorsProliferating Cell Nuclear AntigenChromatinCREB-Binding ProteinDNADNA-Directed DNA Polymerasep300-CBP-Associated Factorp300-CBP Transcription FactorsProliferating Cell Nuclear Antigen

Identifiers

PMID24939902
PMCPMC4117764
OpenAlexW2129240720

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.