Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets
Ruiqi Liu,
Jiajun Wu,
Haiwei Guo,
Weiping Yao,
Shuang Li,
Yanwei Lu,
Yongshi Jia,
Xiaodong Liang,
Jianming Tang,
Haibo Zhang
Affiliations
Ruiqi Liu
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Jiajun Wu
Graduate Department Bengbu Medical College, Bengbu Anhui China
Haiwei Guo
Otolaryngology & Head and Neck Center Cancer Center Department of Head and Neck Surgery Zhejiang Provincial People's Hospital Affiliated People's Hospital, Hangzhou Medical College Hangzhou Zhejiang China
Weiping Yao
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Shuang Li
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Yanwei Lu
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Yongshi Jia
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Xiaodong Liang
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Jianming Tang
Department of Radiation Oncology The First Hospital of Lanzhou University Lanzhou University Lanzhou Gansu China
Haibo Zhang
Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
Abstract 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.