Evidence map›Paper›PMID 16397295›Full record

ArticleNucleic acids research2006

XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage.

Nicolas Lévy, Adeline Martz, Anne Bresson, Catherine Spenlehauer, Gilbert de Murcia, Josiane Ménissier-de Murcia

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
4.8field-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

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 115 citations in OpenAlex.

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  7. Age- and Gender-Independent Association ofInternational journal of general medicine · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Nicolas LévyDépartement Intégrité du génome de l'UMR 7175, CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard S. Brant, BP 10413, F-67412 Illkirch Cedex, France.
Adeline Martz
Anne Bresson
Catherine Spenlehauer
Gilbert de Murcia
Josiane Ménissier-de Murcia
École Supérieure de Biotechnologie de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The two BRCT domains (BRCT1 and BRCT2) of XRCC1 mediate a network of protein-protein interactions with several key factors of the DNA single-strand breaks (SSBs) and base damage repair pathways. BRCT1 is required for the immediate poly(ADP-ribose)-dependent recruitment of XRCC1 to DNA breaks and is essential for survival after DNA damage. To better understand the biological role of XRCC1 in the processing of DNA ends, a search for the BRCT1 domain-associated proteins was performed by mass spectrometry of GST-BRCT1 pulled-down proteins from HeLa cell extracts. Here, we report that the double-strand break (DSB) repair heterotrimeric complex DNA-PK interacts with the BRCT1 domain of XRCC1 and phosphorylates this domain at serine 371 after ionizing irradiation. This caused XRCC1 dimer dissociation. The XRCC1 R399Q variant allele did not affect this phosphorylation. We also show that XRCC1 strongly stimulates the phosphorylation of p53-Ser15 by DNA-PK. The pseudo phosphorylated S371D mutant was a much weaker stimulator of DNA-PK activity whereas the non-phosphorylable mutant S371L endowed with a DNA-PK stimulating capacity failed to fully rescue the DSB repair defect of XRCC1-deficient EM9 rodent cells. The functional association between XRCC1 and DNA-PK in response to IR provides the first evidence for their involvement in a common DSB repair pathway.

Indexed as

DNA DamageDNA RepairAnimalsBinding SitesCricetinaeDimerizationDNA-Activated Protein KinaseDNA-Binding ProteinsHeLa CellsHumansMass SpectrometryPhosphorylationProtein Structure, TertiaryRadiation, IonizingSerineX-ray Repair Cross Complementing Protein 1DNA-Activated Protein KinaseDNA-Binding ProteinsSerineX-ray Repair Cross Complementing Protein 1XRCC1 protein, human

Identifiers

PMID16397295
PMCPMC1325201
OpenAlexW2007784993

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.