Evidence map›Paper›PMID 36537216›Full record

ArticleNucleic acids research2023

The histone acetyltransferase KAT6A is recruited to unmethylated CpG islands via a DNA binding winged helix domain.

Lisa Marie Weber, Yulin Jia, Bastian Stielow, Stephen S Gisselbrecht, Yinghua Cao, Yanpeng Ren, Iris Rohner, Jessica King, Elisabeth Rothman, Sabrina Fischer and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  7. Review
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  10. A multivalent engagement of ENL with MOZ.Nature structural & molecular biology · 2025
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. HBO1, a MYSTerious KAT and its links to cancer.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  18. 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

17 authors at 4 institutions in 3 countries.

Lisa Marie WeberInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.
Yulin JiaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing 100875, China.
Bastian StielowInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.
Stephen S GisselbrechtDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Yinghua CaoKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing 100875, China.
Yanpeng RenKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing 100875, China.
Iris RohnerInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.
Jessica KingDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Elisabeth RothmanDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Sabrina FischerInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.
Clara SimonInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.
Ignasi FornéProtein Analysis Unit, Biomedical Center (BMC), Faculty of Medicine, Ludwig-Maximilians-University (LMU) Munich, Martinsried 82152, Germany.
Andrea NistGenomics Core Facility, Institute of Molecular Oncology, Member of the German Center for Lung Research (DZL), Philipps University of Marburg, Marburg 35043, Germany.
Thorsten StieweGenomics Core Facility, Institute of Molecular Oncology, Member of the German Center for Lung Research (DZL), Philipps University of Marburg, Marburg 35043, Germany.
Martha L BulykDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Zhanxin WangKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing 100875, China.
Robert LiefkeInstitute of Molecular Biology and Tumor Research (IMT), Philipps University of Marburg, Marburg 35043, Germany.ORCID 0000-0002-8549-637X
Philipps University of Marburg · DEBeijing Normal University · CNBrigham and Women's Hospital · USCenter for Integrated Protein Science Munich · DE

Funding

Impact of Coding Variation on Transcription Factor - DNA Recognition_Diversity SupplementR01HG010501 · NHGRI · BRIGHAM AND WOMEN'S HOSPITAL · PI MARTHA L BULYK · 2019 to 2026
$6.9M
NHGRI NIH HHS R01 HG010501
6 · The paper itself

Abstract

The lysine acetyltransferase KAT6A (MOZ, MYST3) belongs to the MYST family of chromatin regulators, facilitating histone acetylation. Dysregulation of KAT6A has been implicated in developmental syndromes and the onset of acute myeloid leukemia (AML). Previous work suggests that KAT6A is recruited to its genomic targets by a combinatorial function of histone binding PHD fingers, transcription factors and chromatin binding interaction partners. Here, we demonstrate that a winged helix (WH) domain at the very N-terminus of KAT6A specifically interacts with unmethylated CpG motifs. This DNA binding function leads to the association of KAT6A with unmethylated CpG islands (CGIs) genome-wide. Mutation of the essential amino acids for DNA binding completely abrogates the enrichment of KAT6A at CGIs. In contrast, deletion of a second WH domain or the histone tail binding PHD fingers only subtly influences the binding of KAT6A to CGIs. Overexpression of a KAT6A WH1 mutant has a dominant negative effect on H3K9 histone acetylation, which is comparable to the effects upon overexpression of a KAT6A HAT domain mutant. Taken together, our work revealed a previously unrecognized chromatin recruitment mechanism of KAT6A, offering a new perspective on the role of KAT6A in gene regulation and human diseases.

Indexed as

ChromatinHistone AcetyltransferasesHistonesAcetylationCpG IslandsDNAHumansChromatinDNAHistone AcetyltransferasesHistonesKAT6A protein, human

Identifiers

PMID36537216
PMCPMC9881136
OpenAlexW4312019858

What OpenQuestion holds

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LicenceCC BY-NC
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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.