Evidence map›Paper›PMID 23307557›Full record

ArticleNucleic acids research2013

p300-mediated acetylation of TRF2 is required for maintaining functional telomeres.

Yoon Ra Her, In Kwon Chung

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. The Intra- and Extra-Telomeric Role of TRF2 in the DNA Damage Response.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Epigenetic features of human telomeres.Nucleic acids research · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Transcriptional outcome of telomere signalling.Nature reviews. Genetics · 2014
    Review
  18. Article
  19. Beyond Telomerase: Telomere Instability as a Novel Target for Cancer Therapy.Journal of molecular and genetic medicine : an international journal of biomedical research · 2013
    Article
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

2 authors at 1 institution in 1 country.

Yoon Ra HerDepartments of Systems Biology and Integrated Omics for Biomedical Science, WCU Program of Graduate School, Yonsei University, Seoul 120-749, Korea.
In Kwon Chung
Yonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human telomeric protein TRF2 is required to protect chromosome ends by facilitating their organization into the protective capping structure. Post-translational modifications of TRF2 such as phosphorylation, ubiquitination, SUMOylation, methylation and poly(ADP-ribosyl)ation have been shown to play important roles in telomere function. Here we show that TRF2 specifically interacts with the histone acetyltransferase p300, and that p300 acetylates the lysine residue at position 293 of TRF2. We also report that p300-mediated acetylation stabilizes the TRF2 protein by inhibiting its ubiquitin-dependent proteolysis and is required for efficient telomere binding of TRF2. Furthermore, overexpression of the acetylation-deficient mutant, K293R, induces DNA-damage response foci at telomeres, thereby leading to induction of impaired cell growth, cellular senescence and altered cell cycle distribution. A small but significant number of metaphase chromosomes show no telomeric signals at chromatid ends, suggesting an aberrant telomere structure. These findings demonstrate that acetylation of TRF2 by p300 plays a crucial role in the maintenance of functional telomeres as well as in the regulation of the telomere-associated DNA-damage response, thus providing a new route for modulating telomere protection function.

Indexed as

AcetylationAmino Acid SubstitutionCell LineCell ProliferationDNA DamageHumansp300-CBP-Associated Factorp300-CBP Transcription FactorsProtein Structure, TertiaryProteolysisTelomereTelomeric Repeat Binding Protein 2Ubiquitinp300-CBP-Associated Factorp300-CBP Transcription FactorsTelomeric Repeat Binding Protein 2TERF2 protein, humanUbiquitin

Identifiers

PMID23307557
PMCPMC3575801
OpenAlexW2140311257

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.