Ubiquitination and deubiquitination in cancer: from mechanisms to novel therapeutic approaches.
Mol Cancer
; 23(1): 148, 2024 Jul 25.
Article
en En
| MEDLINE
| ID: mdl-39048965
ABSTRACT
Ubiquitination, a pivotal posttranslational modification of proteins, plays a fundamental role in regulating protein stability. The dysregulation of ubiquitinating and deubiquitinating enzymes is a common feature in various cancers, underscoring the imperative to investigate ubiquitin ligases and deubiquitinases (DUBs) for insights into oncogenic processes and the development of therapeutic interventions. In this review, we discuss the contributions of the ubiquitin-proteasome system (UPS) in all hallmarks of cancer and progress in drug discovery. We delve into the multiple functions of the UPS in oncology, including its regulation of multiple cancer-associated pathways, its role in metabolic reprogramming, its engagement with tumor immune responses, its function in phenotypic plasticity and polymorphic microbiomes, and other essential cellular functions. Furthermore, we provide a comprehensive overview of novel anticancer strategies that leverage the UPS, including the development and application of proteolysis targeting chimeras (PROTACs) and molecular glues.
Palabras clave
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Complejo de la Endopetidasa Proteasomal
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Ubiquitinación
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Enzimas Desubicuitinizantes
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Neoplasias
Idioma:
En
Revista:
Mol Cancer
Asunto de la revista:
NEOPLASIAS
Año:
2024
Tipo del documento:
Article