Evidence map›Paper›PMID 25301942›Full record

ArticleThe Journal of biological chemistry2014

Regulation of histone acetyltransferase TIP60 function by histone deacetylase 3.

Jingjie Yi, Xiangyang Huang, Yuxia Yang, Wei-Guo Zhu, Wei Gu, Jianyuan Luo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  9. Article
  10. Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  11. Review
  12. The application of histone deacetylases inhibitors in glioblastoma.Journal of experimental & clinical cancer research : CR · 2020
    Review
  13. Review
  14. TIP60 up-regulates ΔNp63α to promote cellular proliferation.The Journal of biological chemistry · 2019
    Article
  15. Article
  16. Review
  17. Article
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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

6 authors at 3 institutions in 2 countries.

Jingjie YiFrom the School of Life Sciences, Xiamen University, Xiamen, Fujian 361005, China, the Department of Medical and Research Technology and Department of Pathology, Program in Oncology, Marlene and Stewart Greenebaum Cancer Center, School of Medicine, University of Maryland, Baltimore, Maryland 21201.
Xiangyang Huangthe Department of Medical and Research Technology and Department of Pathology, Program in Oncology, Marlene and Stewart Greenebaum Cancer Center, School of Medicine, University of Maryland, Baltimore, Maryland 21201, the Department of Rheumatology, West China Hospital, West China School of Medicine, Sichuan University, Chengdu, Sichuan 610041, China, and.
Yuxia Yangthe Peking University Health Science Center, Beijing 100191, China.
Wei-Guo Zhuthe Peking University Health Science Center, Beijing 100191, China.
Wei Guthe Institute for Cancer Genetics and Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, New York 10032.
Jianyuan Luothe Department of Medical and Research Technology and Department of Pathology, Program in Oncology, Marlene and Stewart Greenebaum Cancer Center, School of Medicine, University of Maryland, Baltimore, Maryland 21201, the Peking University Health Science Center, Beijing 100191, China, JLuo@som.umaryland.edu.
Peking University · CNUniversity of Maryland, Baltimore · USCancer Genetics (United States) · US

Funding

PW1--A mediator of cell survival by NFKB and cell death by p53P01CA080058 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI AARONSON, STUART A · 2000 to 2016
$20.2M
Role of p53-mediated unconventional functions in tumor suppressionR01CA172023 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GU, WEI · 2012 to 2016
$1.6M
Regulation of Mdmx stability and subcellular localization by ubiquitinationR01CA166294 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GU, WEI · 2012 to 2016
$1.5M
NCI NIH HHS 2P01CA080058NCI NIH HHS 5R01 CA166294NCI NIH HHS 5R01CA172023NCI NIH HHS R01 CA166294NCI NIH HHS R01 CA172023
6 · The paper itself

Abstract

The key member of the MOZ (monocyticleukaemia zinc finger protein), Ybf2/Sas3, Sas2, and TIP60 acetyltransferases family, Tat-interactive protein, 60 kD (TIP60), tightly modulates a wide array of cellular processes, including chromatin remodeling, gene transcription, apoptosis, DNA repair, and cell cycle arrest. The function of TIP60 can be regulated by SIRT1 through deacetylation. Here we found that TIP60 can also be functionally regulated by HDAC3. We identified six lysine residues as its autoacetylation sites. Mutagenesis of these lysines to arginines completely abolishes the autoacetylation of TIP60. Overexpression of HDAC3 increases TIP60 ubiquitination levels. However, unlike SIRT1, HDAC3 increased the half-life of TIP60. Further study found that HDAC3 colocalized with TIP60 both in the nucleus and the cytoplasm, which could be the reason why HDAC3 can stabilize TIP60. The deacetylation of TIP60 by both SIRT1 and HDAC3 reduces apoptosis induced by DNA damage. Knockdown of HDAC3 in cells increased TIP60 acetylation levels and increased apoptosis after DNA damage. Together, our findings provide a better understanding of TIP60 regulation mechanisms, which is a significant basis for further studies of its cellular functions.

Indexed as

DNA RepairProtein Processing, Post-TranslationalAcetylationAmino Acid SequenceApoptosisCell Line, TumorCell NucleusCytoplasmDNA DamageHalf-LifeHistone AcetyltransferasesHistone Deacetylase 3Histone DeacetylasesHumansLysineLysine Acetyltransferase 5Histone AcetyltransferasesHistone Deacetylase 3Histone DeacetylasesKAT5 protein, humanLysineLysine Acetyltransferase 5RNA, Small InterferingSIRT1 protein, humanSirtuin 1ApoptosisDNA DamageHistone AcetylaseHistone Deacetylase 3 (HDAC3)Ubiquitylation (Ubiquitination)

Identifiers

PMID25301942
PMCPMC4256327
OpenAlexW1980469423

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.