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Ubiquitin specific peptidases and prostate cancer

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 f...

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Autores principales: Guo, Yunfei, Cui, Shuaishuai, Chen, Yuanyuan, Guo, Song, Chen, Dahu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9939025/
https://www.ncbi.nlm.nih.gov/pubmed/36811009
http://dx.doi.org/10.7717/peerj.14799
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author Guo, Yunfei
Cui, Shuaishuai
Chen, Yuanyuan
Guo, Song
Chen, Dahu
author_facet Guo, Yunfei
Cui, Shuaishuai
Chen, Yuanyuan
Guo, Song
Chen, Dahu
author_sort Guo, Yunfei
collection PubMed
description 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.
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spelling pubmed-99390252023-02-20 Ubiquitin specific peptidases and prostate cancer Guo, Yunfei Cui, Shuaishuai Chen, Yuanyuan Guo, Song Chen, Dahu PeerJ Biochemistry 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. PeerJ Inc. 2023-02-16 /pmc/articles/PMC9939025/ /pubmed/36811009 http://dx.doi.org/10.7717/peerj.14799 Text en ©2023 Guo et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biochemistry
Guo, Yunfei
Cui, Shuaishuai
Chen, Yuanyuan
Guo, Song
Chen, Dahu
Ubiquitin specific peptidases and prostate cancer
title Ubiquitin specific peptidases and prostate cancer
title_full Ubiquitin specific peptidases and prostate cancer
title_fullStr Ubiquitin specific peptidases and prostate cancer
title_full_unstemmed Ubiquitin specific peptidases and prostate cancer
title_short Ubiquitin specific peptidases and prostate cancer
title_sort ubiquitin specific peptidases and prostate cancer
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9939025/
https://www.ncbi.nlm.nih.gov/pubmed/36811009
http://dx.doi.org/10.7717/peerj.14799
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AT chendahu ubiquitinspecificpeptidasesandprostatecancer