The SUMOylation and ubiquitination crosstalk in cancer.


Journal

Journal of cancer research and clinical oncology
ISSN: 1432-1335
Titre abrégé: J Cancer Res Clin Oncol
Pays: Germany
ID NLM: 7902060

Informations de publication

Date de publication:
Nov 2023
Historique:
received: 17 07 2023
accepted: 16 08 2023
medline: 2 11 2023
pubmed: 29 8 2023
entrez: 28 8 2023
Statut: ppublish

Résumé

The cancer occurrence and progression are largely affected by the post-translational modifications (PTMs) of proteins. Currently, it has been shown that the relationship between ubiquitination and SUMOylation is highly complex and interactive. SUMOylation affects the process of ubiquitination and degradation of substrates. Contrarily, SUMOylation-related proteins are also regulated by the ubiquitination process thus altering their protein levels or activity. Emerging evidence suggests that the abnormal regulation between this crosstalk may lead to tumorigenesis. In this review, we have discussed the study of the relationship between ubiquitination and SUMOylation, as well as the possibility of a corresponding application in tumor therapy. The relevant literatures from PubMed have been reviewed for this article. The interaction between ubiquitination and SUMOylation is crucial for the occurrence and development of cancer. A greater understanding of the crosstalk of SUMOylation and ubiquitination may be more conducive to the development of more selective and effective SUMOylation inhibitors, as well as a promotion of synergy with other tumor treatment strategies.

Sections du résumé

BACKGROUND BACKGROUND
The cancer occurrence and progression are largely affected by the post-translational modifications (PTMs) of proteins. Currently, it has been shown that the relationship between ubiquitination and SUMOylation is highly complex and interactive. SUMOylation affects the process of ubiquitination and degradation of substrates. Contrarily, SUMOylation-related proteins are also regulated by the ubiquitination process thus altering their protein levels or activity. Emerging evidence suggests that the abnormal regulation between this crosstalk may lead to tumorigenesis.
PURPOSE OBJECTIVE
In this review, we have discussed the study of the relationship between ubiquitination and SUMOylation, as well as the possibility of a corresponding application in tumor therapy.
METHODS METHODS
The relevant literatures from PubMed have been reviewed for this article.
CONCLUSION CONCLUSIONS
The interaction between ubiquitination and SUMOylation is crucial for the occurrence and development of cancer. A greater understanding of the crosstalk of SUMOylation and ubiquitination may be more conducive to the development of more selective and effective SUMOylation inhibitors, as well as a promotion of synergy with other tumor treatment strategies.

Identifiants

pubmed: 37640846
doi: 10.1007/s00432-023-05310-z
pii: 10.1007/s00432-023-05310-z
doi:

Substances chimiques

Proteins 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

16123-16146

Subventions

Organisme : Natural Science Foundation of Ningbo
ID : No.2022J040
Organisme : Natural Science Foundation of Ningbo
ID : No.2022J230
Organisme : Natural Science Foundation of Ningbo
ID : No.2021J065
Organisme : National Natural Science Foundation of China
ID : 32270821
Organisme : Fundamental Research Funds for the Provincial Universities of Zhejiang,
ID : No. SJLZ2022004

Informations de copyright

© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.

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Auteurs

Kailang Li (K)

Department of Oncology, The First Hospital of Ningbo University, Ningbo, 315020, China.
Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathophysiology, Health Science Center, Ningbo University, Ningbo, 315211, China.

Yongming Xia (Y)

Department of Oncology, Yuyao People's Hospital of Zhejiang, Yuyao, 315400, Zhejiang, China.

Jian He (J)

Department of Oncology, The First Hospital of Ningbo University, Ningbo, 315020, China.
Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathophysiology, Health Science Center, Ningbo University, Ningbo, 315211, China.

Jie Wang (J)

Department of Oncology, The First Hospital of Ningbo University, Ningbo, 315020, China.
Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathophysiology, Health Science Center, Ningbo University, Ningbo, 315211, China.

Jingyun Li (J)

Department of Oncology, The First Hospital of Ningbo University, Ningbo, 315020, China.
Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathophysiology, Health Science Center, Ningbo University, Ningbo, 315211, China.

Meng Ye (M)

Department of Oncology, The First Hospital of Ningbo University, Ningbo, 315020, China. yemeng@nbu.edu.cn.
Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathophysiology, Health Science Center, Ningbo University, Ningbo, 315211, China. yemeng@nbu.edu.cn.

Xiaofeng Jin (X)

Department of Oncology, The First Hospital of Ningbo University, Ningbo, 315020, China. jinxiaofeng@nbu.edu.cn.
Department of Biochemistry and Molecular Biology, Zhejiang Key Laboratory of Pathophysiology, Health Science Center, Ningbo University, Ningbo, 315211, China. jinxiaofeng@nbu.edu.cn.

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