REVIEW article
Front. Pharmacol.
Sec. Experimental Pharmacology and Drug Discovery
Volume 16 - 2025 | doi: 10.3389/fphar.2025.1629709
Spotlight on USP30：Structure, Function, Disease and Target Inhibition
Provisionally accepted
- 1College of Pharmacy, Dalian Medical University, Dalian, China
- 2Dalian Medical University, Dalian, China
- 3Zigong Maternal and Child Health Care Hospital, Zigong, China
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This review comprehensively summarizes the current understanding of ubiquitinspecific protease 30 (USP30), covering its structural characteristics, functions in cellular processes, associations with diseases, diagnostic and therapeutic strategies, as well as controversies and future perspectives. USP30, a deubiquitinating enzyme, plays crucial roles in mitochondrial quality control, autophagy regulation, and cellular homeostasis. It is implicated in the progression of several malignancies, including hepatocellular carcinoma, breast carcinoma, and glioblastoma, as well as neurodegenerative disorders such as Parkinson's disease. This involvement is mediated through its regulation of mitochondrial autophagy, stabilization of oncoproteins like Snail and c-Myc, and facilitation of metabolic reprogramming. Inhibition of USP30 has demonstrated potential in reversing the malignant phenotype of tumors and enhancing neuroprotection, highlighting its promise as a versatile therapeutic target. Pharmacological inhibition of USP30, using agents such as S3, MF-094, and FT3967385, enhances ubiquitination and reactivates mitophagy, indicating potential therapeutic benefits in preclinical models. The development of USP30-targeted therapies holds promise but also faces challenges. Further research on USP30 is expected to provide new insights into disease mechanisms and therapeutic interventions.
Keywords: USP30, Target inhibition, Disease, signaling pathway, Structure
Received: 16 May 2025; Accepted: 05 Aug 2025.
Copyright: © 2025 Chu, Du, Gao, Xue, Yang and Duan. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Peng Chu, College of Pharmacy, Dalian Medical University, Dalian, China
Ying Yang, Dalian Medical University, Dalian, China
Xingping Duan, Zigong Maternal and Child Health Care Hospital, Zigong, China
Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.