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Non-Histone Lysine Modifications in Tumor Microenvironment: Mechanisms and Therapeutic Opportunities

Year: 2025
Type: article
Abstract: Post-translational modifications (PTMs) on protein lysine residues, including lactylation, methylation, acetylation, ubiquitination, and succinylation, serve as critical regulators in tumorigenesis and progression. Histone PTMs participate in tumor development by modulating chromatin structure and regulating gene expression. Notably, accumulating evidence reveals that PTMs target extensive non-histone substrates. These modifications occurring on non-histone proteins also contribute to tumor-associated biological processes. In this review, we systematically summarize the impact of non-histone PTMs on tumor and the tumor immune microenvironment (TIME). Additionally, we discuss crosstalk between distinct PTMs, which complicates the regulatory mechanisms of protein function. An in-depth research on PTMs in tumors holds new insights for exploring promising clinical therapeutic strategies.
Authors: Kai Sun, Shuying Xiao, Qibo Huang, Suhang Zhang, Qilin Li, Chuanyu Hu
Language: English
Open Access status: gold
Estimated APC paid: $3,499
OpenAlex ID: W4416419500
FWCI: 0.522
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Cited by: 2
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