Evidence map›Paper›PMID 28069995›Full record

ArticleNucleic acids research2017

ATM induces MacroD2 nuclear export upon DNA damage.

Barbara Golia, Giuliana Katharina Moeller, Gytis Jankevicius, Andreas Schmidt, Anna Hegele, Julia Preißer, Mai Ly Tran, Axel Imhof, Gyula Timinszky

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. ADP-ribosylhydrolases: from DNA damage repair to COVID-19.Journal of Zhejiang University. Science. B · 2021
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Oncotarget · 2018
    Article
  14. Article
  15. 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

9 authors at 1 institution in 1 country.

Barbara GoliaDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Giuliana Katharina MoellerDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Gytis JankeviciusDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Andreas SchmidtZentrallabor für Proteinanalytik (Protein Analysis Unit), Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Anna HegeleDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Julia PreißerDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Mai Ly TranDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Axel ImhofZentrallabor für Proteinanalytik (Protein Analysis Unit), Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany.
Gyula TiminszkyDepartment of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-Universität München, Planegg-Martinsried 82152, Germany gyula.timinszky@med.uni-muenchen.de.
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP-ribosylation is a dynamic post-translation modification that regulates the early phase of various DNA repair pathways by recruiting repair factors to chromatin. ADP-ribosylation levels are defined by the activities of specific transferases and hydrolases. However, except for the transferase PARP1/ARDT1 little is known about regulation of these enzymes. We found that MacroD2, a mono-ADP-ribosylhydrolase, is exported from the nucleus upon DNA damage, and that this nuclear export is induced by ATM activity. We show that the export is dependent on the phosphorylation of two SQ/TQ motifs, suggesting a novel direct interaction between ATM and ADP-ribosylation. Lastly, we show that MacroD2 nuclear export temporally restricts its recruitment to DNA lesions, which may decrease the net ADP-ribosylhydrolase activity at the site of DNA damage. Together, our results identify a novel feedback regulation between two crucial DNA damage-induced signaling pathways: ADP-ribosylation and ATM activation.

Indexed as

DNA DamageProtein Processing, Post-TranslationalActive Transport, Cell NucleusAdenosine DiphosphateAmino Acid MotifsAtaxia Telangiectasia Mutated ProteinsCell Line, TumorCell NucleusDNA Repair EnzymesFeedback, PhysiologicalHeLa CellsHumansHydrolasesOsteoblastsPhosphorylationPoly(ADP-ribose) PolymerasesAdenosine DiphosphateAtaxia Telangiectasia Mutated ProteinsATM protein, humanDNA Repair EnzymesHydrolasesMACROD2 protein, humanPoly(ADP-ribose) Polymerases

Identifiers

PMID28069995
PMCPMC5224513
OpenAlexW2528688991

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.