Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets

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 c...

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Published inMedComm (2020) Vol. 4; no. 3; pp. e292 - n/a
Main Authors Liu, Ruiqi, Wu, Jiajun, Guo, Haiwei, Yao, Weiping, Li, Shuang, Lu, Yanwei, Jia, Yongshi, Liang, Xiaodong, Tang, Jianming, Zhang, Haibo
Format Journal Article
LanguageEnglish
Published China John Wiley & Sons, Inc 01.06.2023
John Wiley and Sons Inc
Wiley
Subjects
acetylation
cancer
Enzymes
methylation
Phosphorylation
post‐translational modifications
Review
Reviews
acetylation
post‐translational modifications
cancer
phosphorylation
methylation
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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. 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.
AbstractList 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.
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.
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.
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.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.
Author Wu, Jiajun
Liu, Ruiqi
Tang, Jianming
Li, Shuang
Jia, Yongshi
Guo, Haiwei
Liang, Xiaodong
Lu, Yanwei
Yao, Weiping
Zhang, Haibo
AuthorAffiliation 1 Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
3 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
2 Graduate Department Bengbu Medical College, Bengbu Anhui China
4 Graduate Department Jinzhou Medical University Jinzhou Liaoning China
5 Department of Radiation Oncology The First Hospital of Lanzhou University Lanzhou University Lanzhou Gansu China
AuthorAffiliation_xml – name: 1 Cancer Center Department of Radiation Oncology Zhejiang Provincial People's Hospital Affiliated People's Hospital Hangzhou Medical College Hangzhou Zhejiang China
– name: 5 Department of Radiation Oncology The First Hospital of Lanzhou University Lanzhou University Lanzhou Gansu China
– name: 4 Graduate Department Jinzhou Medical University Jinzhou Liaoning China
– name: 3 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
– name: 2 Graduate Department Bengbu Medical College, Bengbu Anhui China
Author_xml – sequence: 1
  givenname: Ruiqi
  surname: Liu
  fullname: Liu, Ruiqi
  organization: Bengbu Medical College, Bengbu
– sequence: 2
  givenname: Jiajun
  surname: Wu
  fullname: Wu, Jiajun
  organization: Affiliated People's Hospital, Hangzhou Medical College
– sequence: 3
  givenname: Haiwei
  surname: Guo
  fullname: Guo, Haiwei
  organization: Affiliated People's Hospital, Hangzhou Medical College
– sequence: 4
  givenname: Weiping
  surname: Yao
  fullname: Yao, Weiping
  organization: Bengbu Medical College, Bengbu
– sequence: 5
  givenname: Shuang
  surname: Li
  fullname: Li, Shuang
  organization: Jinzhou Medical University
– sequence: 6
  givenname: Yanwei
  surname: Lu
  fullname: Lu, Yanwei
  organization: Hangzhou Medical College
– sequence: 7
  givenname: Yongshi
  surname: Jia
  fullname: Jia, Yongshi
  organization: Hangzhou Medical College
– sequence: 8
  givenname: Xiaodong
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  email: lxdctopone@sina.com
  organization: Bengbu Medical College, Bengbu
– sequence: 9
  givenname: Jianming
  surname: Tang
  fullname: Tang, Jianming
  email: 15900792812@163.com
  organization: Lanzhou University
– sequence: 10
  givenname: Haibo
  orcidid: 0000-0002-5134-4167
  surname: Zhang
  fullname: Zhang, Haibo
  email: zhanghaibo@hmc.edu.cn
  organization: Hangzhou Medical College
BackLink https://www.ncbi.nlm.nih.gov/pubmed/37220590$$D View this record in MEDLINE/PubMed
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Copyright 2023 The Authors. published by Sichuan International Medical Exchange & Promotion Association (SCIMEA) and John Wiley & Sons Australia, Ltd.
2023 The Authors. MedComm published by Sichuan International Medical Exchange & Promotion Association (SCIMEA) and John Wiley & Sons Australia, Ltd.
2023. This work is published under http://creativecommons.org/licenses/by/4.0/ (the "License"). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
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Issue 3
Keywords acetylation
post‐translational modifications
cancer
phosphorylation
methylation
Language English
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2023 The Authors. MedComm published by Sichuan International Medical Exchange & Promotion Association (SCIMEA) and John Wiley & Sons Australia, Ltd.
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Notes Ruiqi Liu, Jiajun Wu, and Haiwei Guo contributed equally to this study.
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Snippet Histones are DNA‐binding basic proteins found in chromosomes. After the histone translation, its amino tail undergoes various modifications, such as...
Histones are DNA-binding basic proteins found in chromosomes. After the histone translation, its amino tail undergoes various modifications, such as...
Abstract Histones are DNA‐binding basic proteins found in chromosomes. After the histone translation, its amino tail undergoes various modifications, such as...
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SubjectTerms acetylation
cancer
Enzymes
methylation
Phosphorylation
post‐translational modifications
Review
Reviews
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Title Post‐translational modifications of histones: Mechanisms, biological functions, and therapeutic targets
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fmco2.292
https://www.ncbi.nlm.nih.gov/pubmed/37220590
https://www.proquest.com/docview/2826104445
https://www.proquest.com/docview/2818750045
https://pubmed.ncbi.nlm.nih.gov/PMC10200003
https://doaj.org/article/949a5f80866c4f3a9dea03c48a066c67
Volume 4
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