E3 ubiquitin ligases in nasopharyngeal carcinoma and implications for therapies.
E3 ubiquitin ligases
Epstein-Barr virus (EBV)
Nasopharyngeal carcinoma (NPC)
Targeted therapies
Journal
Journal of molecular medicine (Berlin, Germany)
ISSN: 1432-1440
Titre abrégé: J Mol Med (Berl)
Pays: Germany
ID NLM: 9504370
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
08
11
2022
accepted:
14
09
2023
revised:
05
09
2023
medline:
6
12
2023
pubmed:
5
10
2023
entrez:
5
10
2023
Statut:
ppublish
Résumé
Nasopharyngeal carcinoma (NPC) is one of the most common squamous cell carcinomas of the head and neck, and Epstein-Barr virus (EBV) infection is one of the pathogenic factors involved in the oncogenetic development and progression of NPC. E3 ligases, which are key members of the ubiquitin proteasome system (UPS), specifically recognize various oncogenic factors and tumor suppressors and contribute to determining their fate through ubiquitination. Several studies have demonstrated that E3 ligases are aberrantly expressed and mutated in NPC and that these changes are closely associated with the occurrence and progression of NPC. Herein, we aim to thoroughly review the specific action mechanisms by which E3 ligases participate in NPC signaling pathways and discuss their functional relationship with EBV. Moreover, we describe the current progress in and limitations for targeted therapies against E3 ligases in NPC. KEY MESSAGES: • E3 ubiquitin ligases, as members of the UPS system, determine the fate of their substrates and may act either as oncogenic or anti-tumorigenic factors in NPC. • Mutations or dysregulated expression of E3 ubiquitin ligases is closely related to the occurrence, development, and therapeutic sensitivity of NPC, as they play important roles in several signaling pathways affected by EBV infection. • As promising therapeutic targets, E3 ligases may open new avenues for treatment and for improving the prognosis of NPC patients.
Identifiants
pubmed: 37796337
doi: 10.1007/s00109-023-02376-7
pii: 10.1007/s00109-023-02376-7
doi:
Substances chimiques
Ubiquitin-Protein Ligases
EC 2.3.2.27
Ubiquitin
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1543-1565Subventions
Organisme : Natural Science Foundation of Ningbo
ID : 2021J017
Organisme : Natural Science Foundation of Ningbo
ID : 2021J065
Organisme : Natural Science Foundation of Ningbo
ID : 202002N3194
Organisme : The Public Welfare Science and Technology Program Project of Ningbo
ID : 2021S116
Organisme : National Natural Science Foundation of China
ID : 32270821
Organisme : The Fundamental Research Funds for the Provincial Universities of Zhejiang
ID : SJLZ2022004
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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