Wang Xiaoqing, Qu Yu, Li Zhaopei, Xia Qinghua
Department of Pediatric Surgery, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan, Shandong 250021, P.R. China.
Post-doctoral Research Station of Clinical Medicine, Liaocheng People's Hospital, Liaocheng, Shandong 252004, P.R. China.
Mol Clin Oncol. 2025 Mar 11;22(5):39. doi: 10.3892/mco.2025.2834. eCollection 2025 May.
Lysine crotonylation (Kcr) refers to a type of modification in which crotonyl groups are transferred to lysine residues by histone crotonyltransferase (HCT) using crotonyl-coenzyme A (CoA) as a substrate. Kcr is distributed in core histones and in some nonhistone proteins. Histone crotonylation is a newly discovered epigenetic modification with a significant ability to regulate gene expression. Crotonylation occurs on the ε-amino group of lysine residues and results in a modification of the histone charge. Similar to acetylation, the substrate for crotonylation is a donor molecule, crotonyl-CoA, which is linked to the sulfhydryl group of CoA by a thioester bond. Crotonylation is involved in regulating a wide range of biological processes and diseases. With advances in detection technologies, the impact of histone crotonylation on tumors has been revealed. The present review examines the recent discoveries of histone crotonylation, its function in tumors and its regulatory mechanism, which will aid in elucidating the mechanisms of malignant tumor development and provide a theoretical foundation for the development of new targeted cancer therapies.
赖氨酸巴豆酰化（Kcr）是指一种修饰类型，其中巴豆酰基通过组蛋白巴豆酰转移酶（HCT）以巴豆酰辅酶A（CoA）为底物转移至赖氨酸残基上。Kcr分布于核心组蛋白和一些非组蛋白中。组蛋白巴豆酰化是一种新发现的表观遗传修饰，具有显著的调控基因表达的能力。巴豆酰化发生在赖氨酸残基的ε-氨基上，导致组蛋白电荷发生改变。与乙酰化类似，巴豆酰化的底物是供体分子巴豆酰-CoA，它通过硫酯键与CoA的巯基相连。巴豆酰化参与调控广泛的生物学过程和疾病。随着检测技术的进步，组蛋白巴豆酰化对肿瘤的影响已被揭示。本综述探讨了组蛋白巴豆酰化的最新发现、其在肿瘤中的功能及其调控机制，这将有助于阐明恶性肿瘤的发生发展机制，并为开发新的靶向癌症治疗方法提供理论基础。
