Ubiquitin specific peptidases and prostate cancer

• Published in: PeerJ (San Francisco, CA) Vol. 11; p. e14799
• Main Authors: Guo, Yunfei, Cui, Shuaishuai, Chen, Yuanyuan, Guo, Song, Chen, Dahu
• Format: Journal Article
• Language: English
• Published: United States PeerJ. Ltd 16.02.2023; PeerJ, Inc; PeerJ Inc
• Subjects: Amino acids; Androgens; Biochemistry; Cell Biology; Deubiquitination; Enzymes; Gene expression; Humans; Localization; Male; Metastasis; Molecular Biology; Physiology; Post-translation; Post-translational modification; Prostate cancer; Prostatic Neoplasms; Proteases; Protein Processing, Post-Translational; Proteins; Therapeutic targets; Ubiquitin; Ubiquitin - metabolism; Ubiquitin-specific proteases (USPs); Ubiquitin-Specific Proteases - metabolism; Ubiquitination; Prostate cancer; Ubiquitin-specific proteases (USPs); Deubiquitination
• ISSN: 2167-8359; 2167-8359
• DOI: 10.7717/peerj.14799

Protein ubiquitination is an important post-translational modification mechanism, which regulates protein stability and activity. The ubiquitination of proteins can be reversed by deubiquitinating enzymes (DUBs). Ubiquitin-specific proteases (USPs), the largest DUB subfamily, can regulate cellular functions by removing ubiquitin(s) from the target proteins. Prostate cancer (PCa) is the second leading type of cancer and the most common cause of cancer-related deaths in men worldwide. Numerous studies have demonstrated that the development of PCa is highly correlated with USPs. The expression of USPs is either high or low in PCa cells, thereby regulating the downstream signaling pathways and causing the development or suppression of PCa. This review summarized the functional roles of USPs in the development PCa and explored their potential applications as therapeutic targets for PCa.