Post-translational modifications of histones: Mechanisms, biological functions, and therapeutic targets.
Post-translational modifications of histones: Mechanisms, biological functions, and therapeutic targets.
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组蛋白是存在于染色体中的DNA结合碱性蛋白质。组蛋白翻译后，其氨基尾部经历各种修饰，如甲基化、乙酰化、磷酸化、泛素化、丙二酰化、丙酰化、丁酰化、巴豆酰化和乳酸化，它们共同构成“组蛋白密码”。它们的组合与生物学功能的关系可作为一个重要的表观遗传标记。同一组蛋白残基的甲基化和去甲基化、乙酰化和去乙酰化、磷酸化和去磷酸化，甚至不同组蛋白残基之间的甲基化和乙酰化相互协同或拮抗，形成复杂的网络。组蛋白修饰酶是引起组蛋白密码子大量产生的一类酶，已成为肿瘤治疗靶点研究的热点。因此，深入了解组蛋白翻译后修饰（PTM）在细胞生命活动中的作用，对于预防和治疗人类疾病非常重要。本文介绍了几种研究最深入和最新发现的组蛋白翻译后修饰。此外，我们还将重点关注具有致癌潜力的组蛋白修饰酶，它们在各种肿瘤中的异常修饰位点，以及多种重要的分子调控机制。最后，总结了当前研究的不足之处，并指出了未来的研究方向。我们希望提供一个全面的了解，并促进在这一领域的进一步研究。组蛋白尾部会发生多种翻译后修饰。我们已经介绍了组蛋白乙酰化、甲基化、磷酸化、泛素化、丙二酰化、巴豆酰化、丙酰化、丁酰化等。它们通过不同的相关组蛋白位点参与多种生命活动。
Histones are DNA‐binding basic proteins found in chromosomes. After the histone translation, its amino tail undergoes various modifications, such as methylation, acetylation, phosphorylation, ubiquitination, malonylation, propionylation, butyrylation, crotonylation, and lactylation, which together constitute the “histone code.” The relationship between their combination and biological function can be used as an important epigenetic marker. Methylation and demethylation of the same histone residue, acetylation and deacetylation, phosphorylation and dephosphorylation, and even methylation and acetylation between different histone residues cooperate or antagonize with each other, forming a complex network. Histone‐modifying enzymes, which cause numerous histone codes, have become a hot topic in the research on cancer therapeutic targets. Therefore, a thorough understanding of the role of histone post‐translational modifications (PTMs) in cell life activities is very important for preventing and treating human diseases. In this review, several most thoroughly studied and newly discovered histone PTMs are introduced. Furthermore, we focus on the histone‐modifying enzymes with carcinogenic potential, their abnormal modification sites in various tumors, and multiple essential molecular regulation mechanism. Finally, we summarize the missing areas of the current research and point out the direction of future research. We hope to provide a comprehensive understanding and promote further research in this field. Histone tails are subject to a variety of post‐translational modifications. We have introduced histone acetylation, methylation, phosphorylation, ubiquitination, malonylation, crotonylation, propionylation, butyrylation, and so forth. They participate in many life activities through different related histone sites.
影响因子：
3.7
作者：
Tang YA;Wen WL;Chang JW;Wei TT;Tan YH;Salunke S;Chen CT;Chen CS;Wang YC
通讯作者：
Wang YC