Evidence map›Paper›PMID 25950477›Full record

ArticleCell death & disease2015

Acetylation of HDAC1 and degradation of SIRT1 form a positive feedback loop to regulate p53 acetylation during heat-shock stress.

H Yang, B Yan, D Liao, S Huang, Y Qiu

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Histone deacetylases and their inhibitors in kidney diseases.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. The Role of Forkhead Box O in Pathogenesis and Therapy of Diabetes Mellitus.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. P53 in the impaired lungs.DNA repair · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. Hsp90 Stabilizes SIRT1 Orthologs in Mammalian Cells andInternational journal of molecular sciences · 2018
    Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

H YangDepartment of Anatomy and Cell Biology, College of Medicine, University of Florida, Gainsville, FL 32610, USA.
B YanDepartment of Anatomy and Cell Biology, College of Medicine, University of Florida, Gainsville, FL 32610, USA.
D LiaoDepartment of Anatomy and Cell Biology, College of Medicine, University of Florida, Gainsville, FL 32610, USA.
S HuangDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Y QiuDepartment of Anatomy and Cell Biology, College of Medicine, University of Florida, Gainsville, FL 32610, USA.
University of Florida · US

Funding

Regulation of insulator function and globin gene expression by USF and associatedR01HL091929 · NHLBI · UNIVERSITY OF FLORIDA · PI HUANG, SUMING · 2009 to 2013
$2.0M
Transcriptional regulation of TAL1/SCL in normal and malignant hematopoiesisR01HL090589 · NHLBI · UNIVERSITY OF FLORIDA · PI HUANG, SUMING · 2008 to 2012
$1.9M
The role of HDAC1 acetylation on corepressor complex activity and hematopoiesisR01HL095674 · NHLBI · UNIVERSITY OF FLORIDA · PI QIU, YI · 2010 to 2013
$1.4M
NHLBI NIH HHS R01 HL 090589NHLBI NIH HHS R01 HL090589NHLBI NIH HHS R01 HL091929NHLBI NIH HHS R01 HL095674
6 · The paper itself

Abstract

The tumor suppressor p53 is an essential transcription factor that sensitively regulates cellular responses to various stresses. Acetylation, a critically important posttranslational modification of p53, is induced in response to cellular stresses. P53 acetylation level strongly correlates with protein stability and activity. The steady-state level of p53 acetylation is balanced by dynamic acetylation and deacetylation. Despite the function of p53 acetylation being well studied, how the steady state of p53 acetylation level is regulated in response to cellular stresses remains unclear. In particular, the dynamic regulation of the deacetylase activities responsible for p53 deacetylation during cellular stress is unknown. In the current study, we investigated the dynamic regulation of HDAC1 (histone deacetylase 1) and SIRT1 (sirtuin 1), two major enzymes for p53 deacetylation, during cell stress. We found that various cell stress events induce HDAC1 acetylation. The increased level of HDAC1 acetylation correlates with the level of p53 acetylation. Acetylated HDAC1 loses the ability to deacetylate p53. Cellular stresses also promote the decline of the SIRT1 protein in a proteasome-dependent pathway, which also results in the increase of p53 acetylation. Importantly, the decreased level of SIRT1 also contributes to the accumulation of HDAC1 acetylation as SIRT1 deacetylates HDAC1. Therefore, the increase of HDAC1 acetylation and reduced level of SIRT1 protein during cellular stress directly link to the induction of p53 acetylation. These results unveil the mechanism underlying the dynamic regulation of p53 acetylation during cell stress.

Indexed as

AcetylationCell Line, TumorHCT116 CellsHeat-Shock ResponseHistone Deacetylase 1HT29 CellsHumansMCF-7 CellsProtein BindingSirtuin 1Tumor Suppressor Protein p53HDAC1 protein, humanHistone Deacetylase 1SIRT1 protein, humanSirtuin 1TP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID25950477
PMCPMC4669686
OpenAlexW1519248115

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.