The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review

Abstract The balance between ubiquitination and deubiquitination is critical for the degradation, transport, localization, and activity of proteins. Deubiquitinating enzymes (DUBs) greatly contribute to the balance of ubiquitination and deubiquitination, and they have been widely studied due to thei...

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Main Authors: Guang-Fei Yang, Xin Zhang, Yi-Ge Su, Ren Zhao, Yan-Yang Wang
Format: Article
Language:English
Published: BMC 2021-08-01
Series:Cancer Cell International
Subjects:
Online Access:https://doi.org/10.1186/s12935-021-02160-y
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spelling doaj-fc2d4461b8cf4d1283f00abe6bfd96d12021-08-29T11:41:01ZengBMCCancer Cell International1475-28672021-08-0121111110.1186/s12935-021-02160-yThe role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative reviewGuang-Fei Yang0Xin Zhang1Yi-Ge Su2Ren Zhao3Yan-Yang Wang4Dept. of Ultrasound, General Hospital of Ningxia Medical UniversitySchool of Clinical Medicine, Ningxia Medical UniversityGraduate School, Ningxia Medical UniversityDept. of Radiation Oncology, General Hospital of Ningxia Medical UniversityDept. of Radiation Oncology, General Hospital of Ningxia Medical UniversityAbstract The balance between ubiquitination and deubiquitination is critical for the degradation, transport, localization, and activity of proteins. Deubiquitinating enzymes (DUBs) greatly contribute to the balance of ubiquitination and deubiquitination, and they have been widely studied due to their fundamental role in cancer. DUB3/ubiquitin-specific protease 17 (USP17) is a type of DUB that has attracted much attention in cancer research. In this review, we summarize the biological functions and regulatory mechanisms of USP17 in central nervous system, head and neck, thoracic, breast, gastrointestinal, genitourinary, and gynecologic cancers as well as bone and soft tissue sarcomas, and we provide new insights into how USP17 can be used in the management of cancer.https://doi.org/10.1186/s12935-021-02160-yDUB3/USP17CancerUbiquitinationDeubiquitinating enzymesSignaling pathways
collection DOAJ
language English
format Article
sources DOAJ
author Guang-Fei Yang
Xin Zhang
Yi-Ge Su
Ren Zhao
Yan-Yang Wang
spellingShingle Guang-Fei Yang
Xin Zhang
Yi-Ge Su
Ren Zhao
Yan-Yang Wang
The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review
Cancer Cell International
DUB3/USP17
Cancer
Ubiquitination
Deubiquitinating enzymes
Signaling pathways
author_facet Guang-Fei Yang
Xin Zhang
Yi-Ge Su
Ren Zhao
Yan-Yang Wang
author_sort Guang-Fei Yang
title The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review
title_short The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review
title_full The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review
title_fullStr The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review
title_full_unstemmed The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review
title_sort role of the deubiquitinating enzyme dub3/usp17 in cancer: a narrative review
publisher BMC
series Cancer Cell International
issn 1475-2867
publishDate 2021-08-01
description Abstract The balance between ubiquitination and deubiquitination is critical for the degradation, transport, localization, and activity of proteins. Deubiquitinating enzymes (DUBs) greatly contribute to the balance of ubiquitination and deubiquitination, and they have been widely studied due to their fundamental role in cancer. DUB3/ubiquitin-specific protease 17 (USP17) is a type of DUB that has attracted much attention in cancer research. In this review, we summarize the biological functions and regulatory mechanisms of USP17 in central nervous system, head and neck, thoracic, breast, gastrointestinal, genitourinary, and gynecologic cancers as well as bone and soft tissue sarcomas, and we provide new insights into how USP17 can be used in the management of cancer.
topic DUB3/USP17
Cancer
Ubiquitination
Deubiquitinating enzymes
Signaling pathways
url https://doi.org/10.1186/s12935-021-02160-y
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