Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets
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 t...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2023-06-01
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| Series: | MedComm |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/mco2.292 |
| _version_ | 1827924111028912128 |
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| author | Ruiqi Liu Jiajun Wu Haiwei Guo Weiping Yao Shuang Li Yanwei Lu Yongshi Jia Xiaodong Liang Jianming Tang Haibo Zhang |
| author_facet | Ruiqi Liu Jiajun Wu Haiwei Guo Weiping Yao Shuang Li Yanwei Lu Yongshi Jia Xiaodong Liang Jianming Tang Haibo Zhang |
| author_sort | Ruiqi Liu |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-13T05:06:59Z |
| format | Article |
| id | doaj.art-949a5f80866c4f3a9dea03c48a066c67 |
| institution | Directory Open Access Journal |
| issn | 2688-2663 |
| language | English |
| last_indexed | 2024-03-13T05:06:59Z |
| publishDate | 2023-06-01 |
| publisher | Wiley |
| record_format | Article |
| series | MedComm |
| spelling | doaj.art-949a5f80866c4f3a9dea03c48a066c672023-06-16T09:40:37ZengWileyMedComm2688-26632023-06-0143n/an/a10.1002/mco2.292Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targetsRuiqi Liu0Jiajun Wu1Haiwei Guo2Weiping Yao3Shuang Li4Yanwei Lu5Yongshi Jia6Xiaodong Liang7Jianming Tang8Haibo Zhang9Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaGraduate Department Bengbu Medical College, Bengbu Anhui ChinaOtolaryngology & 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 ChinaCancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaCancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaCancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaCancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaCancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaDepartment of Radiation Oncology The First Hospital of Lanzhou University Lanzhou University Lanzhou Gansu ChinaCancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang ChinaAbstract 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.https://doi.org/10.1002/mco2.292acetylationcancermethylationphosphorylationpost‐translational modifications |
| spellingShingle | Ruiqi Liu Jiajun Wu Haiwei Guo Weiping Yao Shuang Li Yanwei Lu Yongshi Jia Xiaodong Liang Jianming Tang Haibo Zhang Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets MedComm acetylation cancer methylation phosphorylation post‐translational modifications |
| title | Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets |
| title_full | Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets |
| title_fullStr | Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets |
| title_full_unstemmed | Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets |
| title_short | Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets |
| title_sort | post translational modifications of histones mechanisms biological functions and therapeutic targets |
| topic | acetylation cancer methylation phosphorylation post‐translational modifications |
| url | https://doi.org/10.1002/mco2.292 |
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