Ubiquitin specific peptidases and prostate cancer

Yunfei Guo; Shuaishuai Cui; Yuanyuan Chen; Song Guo; Dahu Chen

doi:10.7717/peerj.14799

Ubiquitin specific peptidases and prostate cancer

PeerJ. 2023 Feb 16:11:e14799. doi: 10.7717/peerj.14799. eCollection 2023.

Authors

Yunfei Guo¹, Shuaishuai Cui¹, Yuanyuan Chen¹, Song Guo¹, Dahu Chen¹

Affiliation

¹ Shandong University of Technology, School of Life Sciences and Medicine, Zibo, Shandong, China.

Abstract

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.

Keywords: Deubiquitination; Prostate cancer; Ubiquitin-specific proteases (USPs).

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Humans
Male
Prostatic Neoplasms*
Protein Processing, Post-Translational
Ubiquitin / metabolism
Ubiquitin-Specific Proteases* / metabolism
Ubiquitination

Substances

Ubiquitin-Specific Proteases
Ubiquitin

Grants and funding

This study was supported by the National Natural Science Foundation of China (81872005). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.