Evidence map›Paper›PMID 40712016›Full record

ArticleScience advances2025

Nonchromatin regulatory functions of the histone variant H2A.B in SWI/SNF genomic deposition.

Xuanzhao Jiang, Jiayu Wen, Mary L Nelson, Yasmin Dijkwel, Bradley Cairns, Uta-Maria Bauer, Gene Hart-Smith, Tatiana A Soboleva, David J Tremethick

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Xuanzhao JiangThe John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0002-1608-3846
Jiayu WenThe John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0003-1249-6456
Mary L NelsonHoward Hughes Medical Institute, Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.ORCID 0000-0003-3958-718X
Yasmin DijkwelThe John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0002-2222-8407
Bradley CairnsHoward Hughes Medical Institute, Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.ORCID 0000-0002-9864-8811
Uta-Maria BauerInstitute for Molecular Biology and Tumor Research, Philipps-University Marburg, BMFZ, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.ORCID 0000-0003-1344-9117
Gene Hart-SmithAustralian Proteome Analysis Facility, Macquarie University, Sydney, NSW 2109, Australia.ORCID 0000-0003-3907-0367
Tatiana A SobolevaThe John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0003-0391-8530
David J TremethickThe John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0001-5274-8078

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
NCI NIH HHS P30 CA042014
6 · The paper itself

Abstract

The replacement of canonical histones with their variant forms enables the dynamic and context-dependent regulation of the mammalian genome. Histone variants also play key roles in various pathological processes including malignancies. Among these, the aberrant expression of the testis-specific histone variant H2A.B contributes to the pathogenesis of Hodgkin lymphoma. The multifunctionality of histone variants is regulated by their posttranslational modifications (PTMs). However, the PTMs of H2A.B and their functional implications are unknown. Here, we demonstrate that the Amino terminus of H2A.B serves as a central hub for a diverse range of gene regulatory protein-protein interactions, orchestrated by phosphorylation and arginine methylation. This includes a mechanism whereby non-chromatin-bound H2A.B associates with SWI/SNF, which limits its access to the genome. Last, we identify phosphorylated H2A.B as a previously uncharacterized marker of active RNA polymerase II transcription start sites. These findings elucidate a central role for H2A.B in genome regulation and highlight the importance of its PTMs in modulating its multifunctional roles.

Indexed as

Chromosomal Proteins, Non-HistoneHistonesTranscription FactorsArginineGene Expression RegulationHumansMethylationPhosphorylationProtein BindingProtein Processing, Post-TranslationalRNA Polymerase IITranscription Initiation SiteArginineChromosomal Proteins, Non-HistoneHistonesRNA Polymerase IITranscription Factors

Identifiers

PMID40712016
PMCPMC12292949

What OpenQuestion holds

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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.