Evidence map›Paper›PMID 31995034›Full record

ArticleeLife2020

SIRT6 is a DNA double-strand break sensor.

Lior Onn, Miguel Portillo, Stefan Ilic, Gal Cleitman, Daniel Stein, Shai Kaluski, Ido Shirat, Zeev Slobodnik, Monica Einav, Fabian Erdel and 2 more

Abstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
–field-weighted citation impact
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

85 citing papers in PubMed.

  1. Trial
  2. Review
  3. Aging and cancer: current understandings and future perspectives.Signal transduction and targeted therapy · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Structural and enzymatic plasticity of SIRT6 deacylase activity.The Journal of biological chemistry · 2025
    Article
  18. Genes as Genome Stabilizers in Pluripotent Stem Cells.Advances in experimental medicine and biology · 2025
    Review
  19. Review
  20. Review

25 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.

Lior OnnDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Miguel PortilloDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Stefan IlicDepartment of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Gal CleitmanDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Daniel SteinDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Shai KaluskiDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Ido ShiratDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Zeev SlobodnikDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Monica EinavDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.
Fabian ErdelDivision of Chromatin Networks, German Cancer Research Center (DKFZ), BioQuant, Heidelberg, Germany.ORCID 0000-0003-2888-7777
Barak AkabayovDepartment of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel.ORCID 0000-0002-3882-2742
Debra ToiberDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva, Israel.ORCID 0000-0002-1465-0130

Funding

Ben Gurion University High-tech, Bio-tech and Chemo-tech scholarshipIsrael Science Foundation 188/17
6 · The paper itself

Abstract

DNA double-strand breaks (DSB) are the most deleterious type of DNA damage. In this work, we show that SIRT6 directly recognizes DNA damage through a tunnel-like structure that has high affinity for DSB. SIRT6 relocates to sites of damage independently of signaling and known sensors. It activates downstream signaling for DSB repair by triggering ATM recruitment, H2AX phosphorylation and the recruitment of proteins of the homologous recombination and non-homologous end joining pathways. Our findings indicate that SIRT6 plays a previously uncharacterized role as a DNA damage sensor, a critical factor in initiating the DNA damage response (DDR). Moreover, other Sirtuins share some DSB-binding capacity and DDR activation. SIRT6 activates the DDR before the repair pathway is chosen, and prevents genomic instability. Our findings place SIRT6 as a sensor of DSB, and pave the road to dissecting the contributions of distinct DSB sensors in downstream signaling.

Indexed as

DNA Breaks, Double-StrandedSirtuinsCell LineDNA RepairHeLa CellsHumansProtein BindingSignal TransductionSIRT6 protein, humanSirtuinscell biologyDNA damageDNA repairDSBhumansensorSIRT6

Identifiers

PMID31995034
PMCPMC7051178

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.