Evidence map›Paper›PMID 38989615›Full record

ArticleNucleic acids research2024

BOD1L mediates chromatin binding and non-canonical function of H3K4 methyltransferase SETD1A.

Takayuki Hoshii, Sota Kikuchi, Tomoya Kujirai, Takeshi Masuda, Tomoko Ito, Satoshi Yasuda, Makoto Matsumoto, Bahityar Rahmutulla, Masaki Fukuyo, Takeshi Murata and 2 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. A novel mutation inFrontiers in neuroscience · 2026
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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

12 authors.

Takayuki HoshiiDepartment of Molecular Oncology, Graduate School of Medicine, Chiba University, Chiba-shi, Chiba 260-8670, Japan.ORCID 0000-0002-5418-1981
Sota KikuchiDepartment of Molecular Oncology, Graduate School of Medicine, Chiba University, Chiba-shi, Chiba 260-8670, Japan.
Tomoya KujiraiLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Takeshi MasudaInstitute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997-0017, Japan.
Tomoko ItoLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
Satoshi YasudaDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba-shi, Chiba 263-8522, Japan.
Makoto MatsumotoDepartment of Molecular Oncology, Graduate School of Medicine, Chiba University, Chiba-shi, Chiba 260-8670, Japan.
Bahityar RahmutullaDepartment of Molecular Oncology, Graduate School of Medicine, Chiba University, Chiba-shi, Chiba 260-8670, Japan.
Masaki FukuyoDepartment of Molecular Oncology, Graduate School of Medicine, Chiba University, Chiba-shi, Chiba 260-8670, Japan.
Takeshi MurataDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba-shi, Chiba 263-8522, Japan.
Hitoshi KurumizakaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.ORCID 0000-0001-7412-3722
Atsushi KanedaDepartment of Molecular Oncology, Graduate School of Medicine, Chiba University, Chiba-shi, Chiba 260-8670, Japan.ORCID 0000-0002-6980-5515

Funding

AMED JP23ama121018AMED P-PROMOTE JP23ama221118Chiba UniversityJST JPMJER1901KAKENHI JP19H03690KAKENHI JP20H05690KAKENHI JP23H05475Kobayashi Foundation for Cancer ResearchNOVARTIS FoundationTakeda Science FoundationUehara Memorial Foundation
6 · The paper itself

Abstract

The H3K4 methyltransferase SETD1A plays an essential role in both development and cancer. However, essential components involved in SETD1A chromatin binding remain unclear. Here, we discovered that BOD1L exhibits the highest correlated SETD1A co-dependency in human cancer cell lines. BOD1L knockout reduces leukemia cells in vitro and in vivo, and mimics the transcriptional profiles observed in SETD1A knockout cells. The loss of BOD1L immediately reduced SETD1A distribution at transcriptional start sites (TSS), induced transcriptional elongation defect, and increased the RNA polymerase II content at TSS; however, it did not reduce H3K4me3. The Shg1 domain of BOD1L has a DNA binding ability, and a tryptophan residue (W104) in the domain recruits SETD1A to chromatin through the association with SETD1A FLOS domain. In addition, the BOD1L-SETD1A complex associates with transcriptional regulators, including E2Fs. These results reveal that BOD1L mediates chromatin and SETD1A, and regulates the non-canonical function of SETD1A in transcription.

Indexed as

ChromatinHistone-Lysine N-MethyltransferaseHistonesAnimalsCell Line, TumorHumansLeukemiaMiceProtein BindingProtein DomainsRNA Polymerase IITranscription, GeneticTranscription Initiation SiteChromatinhistone H3 trimethyl Lys4Histone-Lysine N-MethyltransferaseHistonesRNA Polymerase IISetd1A protein, human

Identifiers

PMID38989615
PMCPMC11381347

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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.