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. 2023 Feb 11;14(2):112. doi: 10.1038/s41419-023-05656-9

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Four core histones, H2A, H2B, H3, and H4, undergo histone modifications at different amino acid sites in response to specific enzymes, including histone methylation, acetylation, citrullination, O-GlcNAcylation, ubiquitination, and lactylation. Differential histone modification modalities and their regulatory enzymes have been shown to play a role in sepsis or endotoxemia caused by LPS. As two of the more thoroughly studied modalities of histone modifications, the regulatory mechanisms of histone methylation, acetylation, and their catalyzing enzymes in sepsis are better explained. MLL, mixed-lineage leukemia 1; MKL1, megakaryocytic leukemia 1; MCP1, monocyte chemotactic protein-1; JMJD3, Jumonji domain-containing protein D3; KM6BH, (K)-specific demethylase 6B; SIRT, sirtuin; HAT, histone acetyltransferases; HADC, histone deacetylases; NF-Κb, nuclear factor-κB; HGMB1, high mobility group box 1; TNF, tumor necrosis factor; IL, interleukin.