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Editorial: Histone modifications in cancer

Year: 2025
Type: editorial
Abstract: Cancer remains one of the most challenging diseases in modern medicine due to its intricate molecular mechanisms. Beyond genetic alterations, epigenetic regulation has emerged as a central determinant of tumor initiation, progression, and therapeutic response. Among epigenetic mechanisms, histone modifications, including methylation, acetylation, lactylation, phosphorylation, and ubiquitination, play pivotal roles in modulating chromatin architecture and gene expression program without altering the underlying DNA sequence. These histone marks are dynamically written, erased, and read by specific histone-modifying enzymes and reader proteins that collectively fine-tune transcriptional activities. Among the best characterized are acetylation, regulated by histone acetyltransferases (HATs) and histone deacetylases (HDACs), and methylation, controlled by histone methyltransferases (HMTs) and demethylases (HDMs). These reversible modifications regulate essential oncogenic pathways, shaping tumor progression, immune escape, and responsiveness to therapy. This Research Topic, Histone Modifications in Cancer, was curated to provide timely insights into the multifaceted roles of histone modifications in cancer biology and their translational potential as therapeutic targets. The collection integrates original research and review articles that advance our understanding of histone-mediated regulatory mechanisms and highlight emerging opportunities for epigenetic intervention in cancer therapy.Histone-modifying enzymes have been increasingly recognized as critical contributors to tumorigenesis and drug resistance through both epigenetic and non-epigenetic mechanisms (Rodrigues et al., 2024;Stief et al., 2020;Wang et al., 2025) We would like to especially thank the contributors to the Research Topic as well as to acknowledge 115 the expert reviewers for their timely, rigorous and constructive evaluation, which together have 116 enriched this collection. 117
Language: English
Open Access status: gold
Estimated APC paid: $3,801
OpenAlex ID: W4416301187
Cites: 7
Cited by: 1
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