Evidence map›Paper›PMID 41679964›Full record

ArticleJournal of biochemistry2026

DAXX promotes SUMOylation of chromatin-trapped DNMT1.

Shota Tanimoto, Teh-Wei Wang, Tomohiro Yabushita, Yoshie Chiba, Chieko Konishi, Akinori Endo, Yasushi Saeki, Susumu Goyama, Makoto Nakanishi, Atsuya Nishiyama

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Shota TanimotoDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Teh-Wei WangDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Tomohiro YabushitaDivision of Cellular Therapy, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Yoshie ChibaDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Chieko KonishiDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Akinori EndoLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, 2-1-6 kamikitazawa, setagaya-ku, Tokyo 156-8506, Japan.
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, 2-1-6 kamikitazawa, setagaya-ku, Tokyo 156-8506, Japan.ORCID 0000-0002-9202-5453
Susumu GoyamaDivision of Molecular Oncology, Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
Makoto NakanishiDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.ORCID 0000-0002-6707-3584
Atsuya NishiyamaDivision of Cancer Cell Biology, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.ORCID 0000-0002-8416-3776

Funding

MEXT KAKENHI 23KJ0718MEXT KAKENHI 24 K02001MEXT KAKENHI 25H01301MEXT KAKENHI JP19h05740
6 · The paper itself

Abstract

The cytosine analogue 5-aza-2'-deoxycytidine (decitabine; DAC) covalently inhibits DNA methyltransferase 1 (DNMT1), the maintenance DNA methyltransferase, and induces SUMOylation of DNA-trapped DNMT1, promoting proteasomal degradation. However, the regulation of DNMT1 SUMOylation and its biological impact remain unclear. Here, using interphase Xenopus egg extracts that reconstitute maintenance DNA methylation in vitro, we identify death domain-associated protein (DAXX) as a regulator of SUMOylation on chromatin-retained, inactive DNMT1. First, adding 5-aza-dCTP, the triphosphate form of decitabine, induced DNMT1 accumulation on chromatin and robust SUMO2/3 conjugation. Chromatin mass spectrometry (CHROMASS) revealed DAXX enrichment on 5-aza-dCTP-treated chromatin in a SUMO-dependent manner, and DAXX depletion suppressed 5-aza-dCTP-induced DNMT1 SUMOylation. Furthermore, GSK-3484862, a non-covalent DNMT1 inhibitor, drove DNMT1 accumulation on chromatin and triggered DAXX-dependent DNMT1 SUMOylation. We also demonstrated that DAXX loss increased decitabine sensitivity in the myeloid leukaemia (AML) cell line THP-1. Together, these findings show that DAXX promotes SUMOylation of DNMT1 trapped on DNA under both covalent and non-covalent trapping conditions.

Indexed as

Adaptor Proteins, Signal TransducingChromatinCo-Repressor ProteinsDNA (Cytosine-5-)-Methyltransferase 1Molecular ChaperonesNuclear ProteinsSumoylationAnimalsDecitabineDNA MethylationHumansXenopus laevisAdaptor Proteins, Signal TransducingChromatinCo-Repressor ProteinsDAXX protein, humanDecitabineDNA (Cytosine-5-)-Methyltransferase 1DNMT1 protein, humanMolecular ChaperonesNuclear ProteinsDAXXDNA methylationDNMT1SUMOXenopus egg extracts

Identifiers

PMID41679964
PMCPMC13112021

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.