Evidence map›Paper›PMID 41168190›Full record

ArticleNature communications2025

Condensation-dependent interactome of a chromatin remodeler underlies tumor suppressor activities.

Yasuhiro Tsukamoto, Atsuki Kawamura, Ayhan Yurtsever, Hidefumi Suzuki, Nichole Marcela Rojas-Chaverra, Hiroki Sato, Daisuke Ino, Takehiko Ichikawa, Weilin Wei, Shojiro Haji and 9 more

Abstract read
In one paragraph

Article in Nature communications, 2025. 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

19 authors.

Yasuhiro TsukamotoDivision of Tumor Dynamics and Regulation, Cancer Research Institute, Kanazawa University, Kanazawa, Japan. ytsukamo@stu.kanazawa-u.ac.jp.ORCID http://orcid.org/0009-0002-6224-146X
Atsuki Kawamura *Department of Histology and Cell Biology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.
Ayhan Yurtsever *Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Hidefumi Suzuki *Department of Molecular Biology, Graduate School of Medical Science, Yokohama City University, Yokohama, Japan.
Nichole Marcela Rojas-ChaverraDivision of Tumor Dynamics and Regulation, Cancer Research Institute, Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0000-0003-1388-6384
Hiroki SatoDivision of Tumor Dynamics and Regulation, Cancer Research Institute, Kanazawa University, Kanazawa, Japan.
Daisuke InoDepartment of Histology and Cell Biology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0000-0002-8112-0746
Takehiko IchikawaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0000-0002-2438-5502
Weilin WeiNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Shojiro HajiDepartment of Medicine and Bioregulatory Science, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.ORCID http://orcid.org/0000-0003-3651-2836
Dominic Chih-Cheng VoonInflammation and Epithelial Plasticity Unit, Cancer Research Institute, Kanazawa University, Kanazawa, Japan.
Akinobu MatsumotoDivision of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.ORCID http://orcid.org/0000-0002-4077-3935
Kunio MatsumotoDivision of Tumor Dynamics and Regulation, Cancer Research Institute, Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0000-0002-6532-4482
Hidehisa TakahashiDepartment of Molecular Biology, Graduate School of Medical Science, Yokohama City University, Yokohama, Japan.ORCID http://orcid.org/0000-0001-7181-9863
Noriyuki KoderaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0000-0003-4880-8423
Takeshi FukumaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0000-0001-8971-6002
Yoshihiro OgawaDepartment of Medicine and Bioregulatory Science, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan. ogawa.yoshihiro.828@m.kyushu-u.ac.jp.ORCID http://orcid.org/0000-0002-0834-2836
Masaaki NishiyamaDepartment of Histology and Cell Biology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Japan.ORCID http://orcid.org/0009-0002-6868-1749
Katsuya SakaiDivision of Tumor Dynamics and Regulation, Cancer Research Institute, Kanazawa University, Kanazawa, Japan. k_sakai@staff.kanazawa-u.ac.jp.ORCID http://orcid.org/0000-0002-0443-1786

Funding

Japan Agency for Medical Research and Development (AMED) JP22gm6310008MEXT | Japan Science and Technology Agency (JST) 19J23485MEXT | Japan Science and Technology Agency (JST) 21K18250MEXT | Japan Science and Technology Agency (JST) JP21H02847MEXT | Japan Science and Technology Agency (JST) JP22H05592
6 · The paper itself

Abstract

Chromatin remodelers are vital for cellular functions like transcription by modulating nucleosome accessibility. Although biological condensates regulate these processes, the contribution of chromatin remodelers to condensation mechanisms remains poorly understood. Here, we examine the role of the E1321 frameshift mutation in CHD1, a chromatin remodeler, which is often targeted in cancers. This mutation truncates CHD1's C-terminus, leading to an oncogenic transcriptome and promoting tumorigenesis. This is due to the loss of an intrinsically disordered region (IDR) crucial for forming CHD1 condensates. These condensates are facilitated by the presence of H3K4me3-modified nucleosomes and RNA, guided to active promoters to regulate gene expression. Furthermore, CHD1 condensates contain long noncoding RNA and histone-modifying proteins, revealing an integral role for CHD1 condensates in epigenetic regulation. Among these components, MLL mutations frequently co-occur with CHD1 mutations in various cancers, suggesting a shared pathway in cancer development. These findings underscore the importance of chromatin remodeler condensation as a regulatory hub in various cellular processes and tumor suppression.

Indexed as

Chromatin Assembly and DisassemblyDNA-Binding ProteinsDNA HelicasesNeoplasmsAnimalsCarcinogenesisCell Line, TumorChromatinEpigenesis, GeneticGene Expression Regulation, NeoplasticHistone-Lysine N-MethyltransferaseHistonesHumansMutationMyeloid-Lymphoid Leukemia ProteinNucleosomesCHD1 protein, humanChromatinDNA-Binding ProteinsDNA HelicasesHistone-Lysine N-MethyltransferaseHistonesKMT2A protein, humanMyeloid-Lymphoid Leukemia ProteinNucleosomes

Identifiers

PMID41168190
PMCPMC12575849

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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.