Evidence map›Paper›PMID 32994220›Full record

ArticleThe Journal of biological chemistry2020

Molecular basis for histone H3 "K4me3-K9me3/2" methylation pattern readout by Spindlin1.

Fan Zhao, Yunan Liu, Xiaonan Su, Ji-Eun Lee, Yutong Song, Daliang Wang, Kai Ge, Juntao Gao, Michael Q Zhang, Haitao Li

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 21% of its field
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

21 citing papers in PubMed, 28 citations in OpenAlex.

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  9. Epigenetic Regulation Via Electrical Forces.Reviews of physiology, biochemistry and pharmacology · 2025
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  12. Contribution of Electrostatic CHJournal of the American Chemical Society · 2024
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  14. The TUDOR domain of SMN is an H3K79Life science alliance · 2023
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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

10 authors at 5 institutions in 2 countries.

Fan ZhaoMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Yunan LiuMOE Key Laboratory of Bioinformatics, Bioinformatics Division, Center for Synthetic and Systems Biology, BNRist, Tsinghua University, Beijing, China.
Xiaonan SuMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Ji-Eun LeeAdipocyte Biology and Gene Regulation Section, Laboratory of Endocrinology and Receptor Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland USA.
Yutong SongMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Daliang WangMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China.
Kai GeAdipocyte Biology and Gene Regulation Section, Laboratory of Endocrinology and Receptor Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland USA.
Juntao GaoMOE Key Laboratory of Bioinformatics, Bioinformatics Division, Center for Synthetic and Systems Biology, BNRist, Tsinghua University, Beijing, China.
Michael Q ZhangMOE Key Laboratory of Bioinformatics, Bioinformatics Division, Center for Synthetic and Systems Biology, BNRist, Tsinghua University, Beijing, China; Department of Biological Sciences Center for Systems Biology, University of Texas at Dallas, Richardson, Texas, USA.
Haitao LiMOE Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China; Tsinghua-Peking Center for Life Sciences, Beijing, China. Electronic address: lht@tsinghua.edu.cn.
Beijing Advanced Sciences and Innovation Center · CNNational Institutes of Health · USTsinghua University · CNCenter for Life Sciences · CNThe University of Texas at Dallas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone recognition by "reader" modules serves as a fundamental mechanism in epigenetic regulation. Previous studies have shown that Spindlin1 is a reader of histone H3K4me3 as well as "K4me3-R8me2a" and promotes transcription of rDNA or Wnt/TCF4 target genes. Here we show that Spindlin1 also acts as a potent reader of histone H3 "K4me3-K9me3/2" bivalent methylation pattern. Calorimetric titration revealed a binding affinity of 16 nm between Spindlin1 and H3 "K4me3-K9me3" peptide, which is one to three orders of magnitude stronger than most other histone readout events at peptide level. Structural studies revealed concurrent recognition of H3K4me3 and H3K9me3/2 by aromatic pockets 2 and 1 of Spindlin1, respectively. Epigenomic profiling studies showed that Spindlin1 colocalizes with both H3K4me3 and H3K9me3 peaks in a subset of genes enriched in biological processes of transcription and its regulation. Moreover, the distribution of Spindlin1 peaks is primarily associated with H3K4me3 but not H3K9me3, which suggests that Spindlin1 is a downstream effector of H3K4me3 generated in heterochromatic regions. Collectively, our work calls attention to an intriguing function of Spindlin1 as a potent H3 "K4me3-K9me3/2" bivalent mark reader, thereby balancing gene expression and silencing in H3K9me3/2-enriched regions.

Indexed as

Amino Acid SequenceBinding SitesCalorimetryCell Cycle ProteinsCrystallography, X-RayDatabases, ProteinEpigenomicsGene ExpressionHistonesHumansHydrogen BondingMethylationMicrotubule-Associated ProteinsMolecular Dynamics SimulationMutagenesis, Site-DirectedPhosphoproteinsCell Cycle ProteinsHistonesMicrotubule-Associated ProteinsPhosphoproteinsspindlincombinatorial readoutcrystal structureepigeneticsgene transcriptionhistone methylationhistone modificationmethylation patternSpindlin1Tudor domainX-ray crystallography

Identifiers

PMID32994220
PMCPMC7864079
OpenAlexW3091707841

What OpenQuestion holds

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LicenceCC BY
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.