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SIRT2 functions as a histone delactylase and inhibits the proliferation and migration of neuroblastoma cells
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Histone lysine acylations are responsible for the regulation of gene transcription which are involved in the crosstalk between metabolism and epigenetics 1 , 2 . Lysine lactylation (Kla) was identified as a new type of histone acylation when breast cancer cells were under hypoxia or macrophages were exposed to bacterial challenge 3 . Similar to other fatty acids, lactate reacts with coenzyme A to form lactyl-CoA, and Kla deposition is then catalyzed by histone acetyltransferase (HAT) p300 from a lactyl-CoA substrate 3 , 4 , but no proteins are known to function as an “eraser” of histone lactylation modification. Sirtuins are a family of NAD + -dependent enzymes capable of removing acyl lysine modifications to dynamically regulate histone acylations in the context of different physiological and pathological cues 1 . A recent study showed that SIRT2 can remove the lactyl group from synthetic peptides related to pyruvate kinase M2 (PKM2) 5 . It is therefore possible that some sirtuins could function as delactylases for histone lactylation modifications.
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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 [13]
The paper’s main text (page not specified) reports that HDAC1–3 and SIRT1–3 delactylate histone peptides and/or purified histones, and says p300 catalyzes histone lysine lactylation. It does not identify MOF or GCN5 as lactyltransferases, so the full claim is not supported by this source. (LLM, conf=0.88)
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Research works printed but not linked: 10
- Wang, M. & Lin, H. Understanding the function of mammalian sirtuins and protein lysine acylation. Annu. Rev. Biochem. 90, 245–285 (2021). · DOI
- Sabari, B. R., Zhang, D., Allis, C. D. & Zhao, Y. Metabolic regulation of gene expression through histone acylations. Nat. Rev. Mol. Cell Biol 18, 90–101 (2017). · DOI
- Zhang, D. et al. Metabolic regulation of gene expression by histone lactylation. Nature 574, 575–580 (2019). · DOI · Paper page
- Heider, J. A new family of CoA-transferases. FEBS Lett. 509, 345–349 (2001). · DOI
- Jennings, E. Q. et al. Sirtuin 2 regulates protein lactoyllys modifications. Chembiochem 22, 2102–2106 (2021). · DOI
- Hang, T. et al. Structural insights into the molecular mechanism underlying Sirt5-catalyzed desuccinylation of histone peptides. Biochem. J. 476, 211–223 (2019). · DOI
- Yu, J. et al. Histone lactylation drives oncogenesis by facilitating m(6)A reader protein YTHDF2 expression in ocular melanoma. Genome Biol. 22, 85 (2021). · DOI
- Louis, C. U. & Shohet, J. M. Neuroblastoma: molecular pathogenesis and therapy. Annu. Rev. Med. 66, 49–63 (2015). · DOI
- Lu, W. et al. SUMOylation is essential for Sirt2 tumor-suppressor function in neuroblastoma. Neoplasia 23, 129–139 (2021). · DOI
- Moreno-Yruela, C. et al. Class I histone deacetylases (HDAC1-3) are histone lysine delactylases. Sci. Adv. 8, eabi6696 (2022). · DOI · Paper page
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Lactylation modification of HIF-1α enhances its stability by blocking VHL recognition
Li, C., Fu, C., Zhou, W., Li, H., Liu, Z., Wu, G., He, T., Shen, M., & Liu, H. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02366-x · Cited by 60
“Ongoing exploration has led to the discovery of delacty-lases and lactyltransferases, with SIRT1-3 and HDAC1-3 identified as histone lysine delactylases and P300/ MOF/GCN5 identified as lactyltransferases [8, 13–15].”
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Metadata
- Authors
- Zu, H., Li, C., Dai, C., Pan, Y., Ding, C., Sun, H., Zhang, X., Yao, X., Zang, J., & Mo, X.
- Affiliations
- University of Science and Technology of China (CN)
- Shanghai Jiao Tong University (CN)
- Zhengzhou University (CN)
- Corresponding author
- Yao, Xuebiao
- Zang, Jianye
- Mo, Xi
- Venue
- Cell Discovery
- Published
- 2022-06-07
- Volume
- 8
- Issue
- 1
- Pages
- 54-54
- ISSN
- 2056-5968 (ISSN-L)
- PMC
- PMC9174446
- OpenAlex
- W4281634015
- Cited by
- 163
- References
- 0
- Citations by year
- 2026: 81 · 2025: 45 · 2024: 26 · 2023: 8 · 2022: 3
- FWCI
- 11.85
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Cell Discovery (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Science and Technology Commission of Shanghai Municipality (18ZR1424500)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- SIRT2, histone lysine lactylation, neuroblastoma, cell proliferation, cell migration, sirtuins, histone acylation, epigenetics
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