Evidence map›Paper›PMID 38709169›Full record

ArticleThe Journal of cell biology2024

ISWI chromatin remodeling complexes recruit NSD2 and H3K36me2 in pericentromeric heterochromatin.

Naoki Goto, Kazuma Suke, Nao Yonezawa, Hidenori Nishihara, Tetsuya Handa, Yuko Sato, Tomoya Kujirai, Hitoshi Kurumizaka, Kazuo Yamagata, Hiroshi Kimura

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Professor Emma Whitelaw, a pioneer of epigenetic inheritance.Frontiers in epigenetics and epigenomics · 2025
    Article
  4. 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

10 authors.

Naoki GotoSchool of Life Science and Technology, Tokyo Institute of Technology , Yokohama, Japan.ORCID 0009-0009-2446-0988
Kazuma SukeFaculty of Biology-Oriented Science and Technology, Kindai University , Kinokawa, Japan.ORCID 0009-0001-4051-1265
Nao YonezawaFaculty of Biology-Oriented Science and Technology, Kindai University , Kinokawa, Japan.ORCID 0009-0007-5162-8833
Hidenori NishiharaSchool of Life Science and Technology, Tokyo Institute of Technology , Yokohama, Japan.ORCID 0000-0002-5843-9994
Tetsuya HandaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology , Yokohama, Japan.ORCID 0000-0001-7707-0195
Yuko SatoSchool of Life Science and Technology, Tokyo Institute of Technology , Yokohama, Japan.ORCID 0000-0002-7805-9171
Tomoya KujiraiInstitute for Quantitative Biosciences, The University of Tokyo , Tokyo, Japan.ORCID 0000-0001-5547-9598
Hitoshi KurumizakaInstitute for Quantitative Biosciences, The University of Tokyo , Tokyo, Japan.ORCID 0000-0001-7412-3722
Kazuo YamagataFaculty of Biology-Oriented Science and Technology, Kindai University , Kinokawa, Japan.ORCID 0000-0002-1716-3442
Hiroshi KimuraSchool of Life Science and Technology, Tokyo Institute of Technology , Yokohama, Japan.ORCID 0000-0003-0854-083X

Funding

Japan Agency for Medical Research and Development JP23ama121020Japan Science and Technology Agency JPMJCR20S6Japan Society for the Promotion of Science JP17H01417
6 · The paper itself

Abstract

Histone H3 lysine36 dimethylation (H3K36me2) is generally distributed in the gene body and euchromatic intergenic regions. However, we found that H3K36me2 is enriched in pericentromeric heterochromatin in some mouse cell lines. We here revealed the mechanism of heterochromatin targeting of H3K36me2. Among several H3K36 methyltransferases, NSD2 was responsible for inducing heterochromatic H3K36me2. Depletion and overexpression analyses of NSD2-associating proteins revealed that NSD2 recruitment to heterochromatin was mediated through the imitation switch (ISWI) chromatin remodeling complexes, such as BAZ1B-SMARCA5 (WICH), which directly binds to AT-rich DNA via a BAZ1B domain-containing AT-hook-like motifs. The abundance and stoichiometry of NSD2, SMARCA5, and BAZ1B could determine the localization of H3K36me2 in different cell types. In mouse embryos, H3K36me2 heterochromatin localization was observed at the two- to four-cell stages, suggesting its physiological relevance.

Indexed as

Chromatin Assembly and DisassemblyHeterochromatinHistone-Lysine N-MethyltransferaseHistonesRepressor ProteinsAdenosine TriphosphatasesAnimalsBromodomain Containing ProteinsCentromereChromosomal Proteins, Non-HistoneHumansMethylationMiceTranscription FactorsAdenosine TriphosphatasesBAZ1B protein, humanBaz1b protein, mouseBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneHeterochromatinHistone-Lysine N-MethyltransferaseHistonesNSD2 protein, humanRepressor ProteinsSMARCA5 protein, humanSmarca5 protein, mouseTranscription FactorsWHSC1 protein, mouse

Identifiers

PMID38709169
PMCPMC11076809

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.