Evidence map›Paper›PMID 33311704›Full record

ArticleExperimental & molecular medicine2020

Histone acylation marks respond to metabolic perturbations and enable cellular adaptation.

Chanhee Jo, Seokjae Park, Sungjoon Oh, Jinmi Choi, Eun-Kyoung Kim, Hong-Duk Youn, Eun-Jung Cho

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

54 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
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  9. The metabolic profiles of cancer stem cells.Stem cell research & therapy · 2026
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  12. Review
  13. Crosstalk BetweenCancers · 2026
    Review
  14. Article
  15. Review
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  17. Epigenetic alterations in Myeloid Malignancies.Advances in experimental medicine and biology · 2026
    Review
  18. Review
  19. Review
  20. 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

7 authors at 3 institutions in 1 country.

Chanhee JoSchool of Pharmacy, Sungkyunkwan University, Suwon, Gyeonggi-do, 440-746, Republic of Korea.
Seokjae ParkDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu, 42988, Republic of Korea.
Sungjoon OhDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu, 42988, Republic of Korea.
Jinmi ChoiSchool of Pharmacy, Sungkyunkwan University, Suwon, Gyeonggi-do, 440-746, Republic of Korea.
Eun-Kyoung KimDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu, 42988, Republic of Korea.
Hong-Duk YounNational Creative Research Center for Epigenome Reprogramming Network, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.ORCID http://orcid.org/0000-0001-9741-8566
Eun-Jung ChoSchool of Pharmacy, Sungkyunkwan University, Suwon, Gyeonggi-do, 440-746, Republic of Korea. echo@skku.edu.ORCID http://orcid.org/0000-0002-6610-5329
Daegu Gyeongbuk Institute of Science and Technology · KRSeoul National University · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylation is the most studied histone acyl modification and has been recognized as a fundamental player in metabolic gene regulation, whereas other short-chain acyl modifications have only been recently identified, and little is known about their dynamics or molecular functions at the intersection of metabolism and epigenetic gene regulation. In this study, we aimed to understand the link between nonacetyl histone acyl modification, metabolic transcriptional regulation, and cellular adaptation. Using antibodies specific for butyrylated, propionylated, and crotonylated H3K23, we analyzed dynamic changes of H3K23 acylation upon various metabolic challenges. Here, we show that H3K23 modifications were highly responsive and reversibly regulated by nutrient availability. These modifications were commonly downregulated by the depletion of glucose and recovered based on glucose or fatty acid availability. Depletion of metabolic enzymes, namely, ATP citrate lyase, carnitine acetyltransferase, and acetyl-CoA synthetase, which are involved in Ac-CoA synthesis, resulted in global loss of H3K23 butyrylation, crotonylation, propionylation, and acetylation, with a profound impact on gene expression and cellular metabolic states. Our data indicate that Ac-CoA/CoA and central metabolic inputs are important for the maintenance of histone acylation. Additionally, genome-wide analysis revealed that acyl modifications are associated with gene activation. Our study shows that histone acylation acts as an immediate and reversible metabolic sensor enabling cellular adaptation to metabolic stress by reprogramming gene expression.

Indexed as

Adaptation, BiologicalEnergy MetabolismAcetyl Coenzyme AAcylationAnimalsCell LineChromatinChromatin Assembly and DisassemblyCoenzyme AEpigenesis, GeneticGas Chromatography-Mass SpectrometryGene Expression RegulationGlucoseHistonesHumansMetabolomeAcetyl Coenzyme AChromatinCoenzyme AGlucoseHistones

Identifiers

PMID33311704
PMCPMC8080766
OpenAlexW3112489042

What OpenQuestion holds

Textmetadata
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.