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USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target
An essential protein regulatory system in cells is the ubiquitin-proteasome pathway. The substrate is modified by the ubiquitin ligase system (E1-E2-E3) in this pathway, which is a dynamic protein bidirectional modification regulation system. Deubiquitinating enzymes (DUBs) are tasked with specifica...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10485055/ https://www.ncbi.nlm.nih.gov/pubmed/37679322 http://dx.doi.org/10.1038/s41420-023-01629-1 |
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author | Li, Shuang Song, Yang Wang, Kexin Liu, Guoxiang Dong, Xiaolei Yang, Fanghao Chen, Guang Cao, Can Zhang, Huhu Wang, Mengjun Li, Ya Zeng, Teng Liu, Chunyan Li, Bing |
author_facet | Li, Shuang Song, Yang Wang, Kexin Liu, Guoxiang Dong, Xiaolei Yang, Fanghao Chen, Guang Cao, Can Zhang, Huhu Wang, Mengjun Li, Ya Zeng, Teng Liu, Chunyan Li, Bing |
author_sort | Li, Shuang |
collection | PubMed |
description | An essential protein regulatory system in cells is the ubiquitin-proteasome pathway. The substrate is modified by the ubiquitin ligase system (E1-E2-E3) in this pathway, which is a dynamic protein bidirectional modification regulation system. Deubiquitinating enzymes (DUBs) are tasked with specifically hydrolyzing ubiquitin molecules from ubiquitin-linked proteins or precursor proteins and inversely regulating protein degradation, which in turn affects protein function. The ubiquitin-specific peptidase 32 (USP32) protein level is associated with cell cycle progression, proliferation, migration, invasion, and other cellular biological processes. It is an important member of the ubiquitin-specific protease family. It is thought that USP32, a unique enzyme that controls the ubiquitin process, is closely linked to the onset and progression of many cancers, including small cell lung cancer, gastric cancer, breast cancer, epithelial ovarian cancer, glioblastoma, gastrointestinal stromal tumor, acute myeloid leukemia, and pancreatic adenocarcinoma. In this review, we focus on the multiple mechanisms of USP32 in various tumor types and show that USP32 controls the stability of many distinct proteins. Therefore, USP32 is a key and promising therapeutic target for tumor therapy, which could provide important new insights and avenues for antitumor drug development. The therapeutic importance of USP32 in cancer treatment remains to be further proven. In conclusion, there are many options for the future direction of USP32 research. |
format | Online Article Text |
id | pubmed-10485055 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-104850552023-09-09 USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target Li, Shuang Song, Yang Wang, Kexin Liu, Guoxiang Dong, Xiaolei Yang, Fanghao Chen, Guang Cao, Can Zhang, Huhu Wang, Mengjun Li, Ya Zeng, Teng Liu, Chunyan Li, Bing Cell Death Discov Review Article An essential protein regulatory system in cells is the ubiquitin-proteasome pathway. The substrate is modified by the ubiquitin ligase system (E1-E2-E3) in this pathway, which is a dynamic protein bidirectional modification regulation system. Deubiquitinating enzymes (DUBs) are tasked with specifically hydrolyzing ubiquitin molecules from ubiquitin-linked proteins or precursor proteins and inversely regulating protein degradation, which in turn affects protein function. The ubiquitin-specific peptidase 32 (USP32) protein level is associated with cell cycle progression, proliferation, migration, invasion, and other cellular biological processes. It is an important member of the ubiquitin-specific protease family. It is thought that USP32, a unique enzyme that controls the ubiquitin process, is closely linked to the onset and progression of many cancers, including small cell lung cancer, gastric cancer, breast cancer, epithelial ovarian cancer, glioblastoma, gastrointestinal stromal tumor, acute myeloid leukemia, and pancreatic adenocarcinoma. In this review, we focus on the multiple mechanisms of USP32 in various tumor types and show that USP32 controls the stability of many distinct proteins. Therefore, USP32 is a key and promising therapeutic target for tumor therapy, which could provide important new insights and avenues for antitumor drug development. The therapeutic importance of USP32 in cancer treatment remains to be further proven. In conclusion, there are many options for the future direction of USP32 research. Nature Publishing Group UK 2023-09-07 /pmc/articles/PMC10485055/ /pubmed/37679322 http://dx.doi.org/10.1038/s41420-023-01629-1 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Review Article Li, Shuang Song, Yang Wang, Kexin Liu, Guoxiang Dong, Xiaolei Yang, Fanghao Chen, Guang Cao, Can Zhang, Huhu Wang, Mengjun Li, Ya Zeng, Teng Liu, Chunyan Li, Bing USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
title | USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
title_full | USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
title_fullStr | USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
title_full_unstemmed | USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
title_short | USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
title_sort | usp32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10485055/ https://www.ncbi.nlm.nih.gov/pubmed/37679322 http://dx.doi.org/10.1038/s41420-023-01629-1 |
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