Evidence map›Paper›PMID 39116123›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome.

Xingyu Liu, Ying Zhang, Zhihui Wen, Yan Hao, Charles A S Banks, Joseph Cesare, Saikat Bhattacharya, Shreyas Arvindekar, Jeffrey J Lange, Yixuan Xie and 7 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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. Article
  3. Metabolic control of glycosylation forms for establishing glycan-dependent protein interaction networks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Xingyu LiuStowers Institute for Medical Research, Kansas City, MO 64110.
Ying ZhangStowers Institute for Medical Research, Kansas City, MO 64110.
Zhihui WenStowers Institute for Medical Research, Kansas City, MO 64110.
Yan HaoStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0001-9186-4821
Charles A S BanksStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0002-0404-2940
Joseph CesareStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0002-5569-1422
Saikat BhattacharyaStowers Institute for Medical Research, Kansas City, MO 64110.
Shreyas ArvindekarNational Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India.ORCID 0000-0002-9945-8534
Jeffrey J LangeStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0003-4970-6269
Yixuan XieDepartment of Biochemistry and Molecular Biophysics, Washington University St. Louis School of Medicine, St. Louis, MO 63110.ORCID 0000-0002-8512-6053
Benjamin A GarciaDepartment of Biochemistry and Molecular Biophysics, Washington University St. Louis School of Medicine, St. Louis, MO 63110.
Brian D SlaughterStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0001-8305-8395
Jay R UnruhStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0003-3077-4990
Shruthi ViswanathNational Centre for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India.ORCID 0000-0002-9061-8407
Laurence FlorensStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0002-9310-6650
Jerry L WorkmanStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0001-8163-1952
Michael P WashburnStowers Institute for Medical Research, Kansas City, MO 64110.ORCID 0000-0001-7568-2585

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Viral modulation of epitranscriptomic mechanismsR01AI118891 · NIAID · WASHINGTON UNIVERSITY · PI GARCIA, BENJAMIN A, WEITZMAN, MATTHEW D. · 2015 to 2025
$5.4M
Transcription regulation in chromatinR35GM118068 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI JERRY L WORKMAN · 2016 to 2026
$4.2M
Quantitative mass spectrometry for comprehending epigenetic mechanisms in a new underlying neurological developmental disorderR01HD106051 · NICHD · WASHINGTON UNIVERSITY · PI Benjamin A Garcia · 2022 to 2026
$2.6M
Decoding the Assembly and Function of Paralogue Specific SIN3A and SIN3B Human Chromatin Remodeling Complexes and NetworksR35GM145240 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI MICHAEL P WASHBURN · 2022 to 2026
$1.9M
Kansas Medical Scientist Training ProgramT32GM138077 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI TIMOTHY A FIELDS · 2020 to 2026
$1.6M
Department of Atomic Energy, Government of India (DAE) DAE TIFR RTI 4006HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM118068HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM145240NCI NIH HHS P01 CA196539NIAID NIH HHS R01 AI118891NICHD NIH HHS R01 HD106051NIGMS NIH HHS R35 GM118068NIGMS NIH HHS R35 GM145240NIGMS NIH HHS T32 GM138077Science Engineering and Research Board, Department of Science and Technology, Government of India SPG/2020/000475Stowers Institute for Medical Research (SIMR) None Available
6 · The paper itself

Abstract

Serial capture affinity purification (SCAP) is a powerful method to isolate a specific protein complex. When combined with cross-linking mass spectrometry and computational approaches, one can build an integrated structural model of the isolated complex. Here, we applied SCAP to dissect a subpopulation of WDR76 in complex with SPIN1, a histone reader that recognizes trimethylated histone H3 lysine4 (H3K4me3). In contrast to a previous SCAP analysis of the SPIN1:SPINDOC complex, histones and the H3K4me3 mark were enriched with the WDR76:SPIN1 complex. Next, interaction network analysis of copurifying proteins and microscopy analysis revealed a potential role of the WDR76:SPIN1 complex in the DNA damage response. Since we detected 149 pairs of cross-links between WDR76, SPIN1, and histones, we then built an integrated structural model of the complex where SPIN1 recognized the H3K4me3 epigenetic mark while interacting with WDR76. Finally, we used the powerful Bayesian Integrative Modeling approach as implemented in the Integrative Modeling Platform to build a model of WDR76 and SPIN1 bound to the nucleosome.

Indexed as

DNA DamageHistonesNucleosomesATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCell Cycle ProteinsDNA HelicasesHumansModels, MolecularProtein BindingATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCell Cycle ProteinsDNA Helicaseshistone H3 trimethyl Lys4HistonesNucleosomesRUVBL2 protein, humanchromatincross-linking mass spectrometryintegrated structural modelingproteomics

Identifiers

PMID39116123
PMCPMC11331135

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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.