The ubiquitin-proteasome system: A potential target for the MASLD.
10.1016/j.apsb.2025.01.010
- Author:
Yue LIU
1
;
Meijia QIAN
1
;
Yonghao LI
1
;
Xin DONG
2
;
Yulian WU
2
;
Tao YUAN
1
;
Jian MA
3
;
Bo YANG
1
;
Hong ZHU
1
;
Qiaojun HE
1
Author Information
1. Institute of Pharmacology & Toxicology, Zhejiang Key Laboratory of Anti-Cancer Drug Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
2. Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310009, China.
3. Center for Drug Safety Evaluation and Research, College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
- Publication Type:Review
- Keywords:
Deubiquitinase (DUB);
E3 ubiquitin ligase;
MASLD;
Neddylation;
SUMOylation;
Therapeutic targets;
Ubiquitin proteasome system (UPS);
Ubiquitination
- From:
Acta Pharmaceutica Sinica B
2025;15(3):1268-1280
- CountryChina
- Language:English
-
Abstract:
Metabolic dysfunction-associated steatotic liver disease (MASLD), the most prevalent chronic liver condition globally, lacks adequate and effective therapeutic remedies in clinical practice. Recent studies have increasingly highlighted the close connection between the ubiquitin-proteasome system (UPS) and the progression of MASLD. This relationship is crucial for understanding the disease's underlying mechanism. As a sophisticated process, the UPS govern protein stability and function, maintaining protein homeostasis, thus influencing a multitude of elements and biological events of eukaryotic cells. It comprises four enzyme families, namely, ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), ubiquitin-protein ligases (E3), and deubiquitinating enzymes (DUBs). This review aims to delve into the array of pathways and therapeutic targets implicated in the ubiquitination within the pathogenesis of MASLD. Therefore, this review unveils the role of ubiquitination in MASLD while spotlighting potential therapeutic targets within the context of this disease.
