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Cited by 841Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

Class I histone deacetylases (HDAC1–3) are histone lysine delactylases

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Moreno-Yruela, Carlos, Zhang, Di, Wei, Wei, Bæk, Michael, Liu, Wenchao, Gao, Jinjun, Danková, Daniela, Nielsen, Alexander L. +6 more·2022·Science Advances
DOI 10.1126/sciadv.abi6696PMC PMC8769552

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Abstract

Abstract Lysine l -lactylation [K( l -la)] is a newly discovered histone mark that can be stimulated under conditions of high glycolysis, such as the Warburg effect. K( l -la) is associated with functions that are different from the widely studied histone acetylation. While K( l -la) can be introduced by the acetyltransferase p300, histone delactylase enzymes remain unknown. Here, we report the systematic evaluation of zinc- and NAD + -dependent HDACs for their ability to cleave ε- N - l -lactyllysine marks. Our screens identified HDACs 1–3 and SIRT1–3 as delactylases in vitro. HDACs 1–3 show robust activity toward not only K( l -la) but also K( d -la) and diverse short-chain acyl modifications. We further confirmed the de- l -lactylase activity of HDACs 1 and 3 in cells. Identification of p300 and HDAC3 as regulatory enzymes suggests that histone lactylation is installed and removed by enzymes as opposed to spontaneous chemical reactivity. Our results therefore represent an important step toward full characterization of this pathway’s regulatory elements.

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  • SIRT1-3 and HDAC1-3 are histone lysine delactylases and P300/MOF/GCN5 are lactyltransferases.

    “with SIRT1-3 and HDAC1-3 identified as histone lysine delactylases and P300/MOF/GCN5 identified as lactyltransferases [8, 13–15].”

    From Lactylation modification of HIF-1α enhances its stability by blocking VHL recognition (2025) · cites this paper as [15]

    The Abstract identifies HDAC1–3 and SIRT1–3 as delactylases in vitro, and the Introduction says p300 can transfer lactyl groups onto histones. The Introduction qualifies SIRT1–3 activity as minor, while the Discussion says their cellular role remains unresolved. Our copy does not identify MOF or GCN5 as lactyltransferases. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

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Authors
Moreno-Yruela, C., Zhang, D., Wei, W., Bæk, M., Liu, W., Gao, J., Danková, D., Nielsen, A. L., Bolding, J. E., Yang, L., Jameson, S. T., Wong, J., Olsen, C. A., & Zhao, Y.
Affiliations
  • Center for Biopharmaceuticals and Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark.
  • University of Chicago (US)
  • East China Normal University (CN)
  • University of Copenhagen (DK)
Corresponding author
  • Zhang, Di
  • Olsen, Christian A.
  • Zhao, Yingming
ORCID
Venue
Science Advances
Publisher
American Association for the Advancement of Science (AAAS)
Published
2022-01-21
Volume
8
Issue
3
Pages
eabi6696-eabi6696
ISSN
2375-2548 (ISSN-L)
DOI
10.1126/sciadv.abi6696
PMC
PMC8769552
OpenAlex
W4220670155
Cited by
841
References
11
Citations by year
2026: 322 · 2025: 262 · 2024: 133 · 2023: 78 · 2022: 41 · 2021: 4 · 2012: 1
FWCI
42.62
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • Science Advances (publishedVersion, cc-by-nc)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by-nc)
  • Knowledge@UChicago (University of Chicago) (submittedVersion, cc-by-nc-nd)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
  • University of Chicago
Funders
  • University of Chicago
  • Danmarks Frie Forskningsfond (6108-00166B, 0136-00412B)
  • National Institutes of Health (HEK293T, 5r01gm135504-03, GM135504, CA251677)
  • National Cancer Institute (R01CA251677)
  • National Institute of General Medical Sciences (R01-GM135504)
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK118266)
  • National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR078555)
  • H2020 European Research Council (725172)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords
histone lysine lactylation, histone deacetylase, HDAC1, HDAC3, HDAC2, SIRT1, SIRT2, SIRT3, Warburg effect, glycolysis, histone modifications, P300
MeSH terms
Acetylation, Histone Deacetylases, Histones, Lysine

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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