The emerging role of ubiquitin-specific protease 20 in tumorigenesis and cancer therapeutics.

Abstract

As a critical member of the ubiquitin-specific proteolytic enzyme family, ubiquitin-specific peptidase 20 (USP20) regulates the stability of proteins via multiple signaling pathways. In addition, USP20 upregulation is associated with various cellular biological processes, such as cell cycle progression, proliferation, migration, and invasion. Emerging studies have revealed the pivotal role of USP20 in the tumorigenesis of various cancer types, such as breast cancer, colon cancer, lung cancer, gastric cancer and adult T cell leukemia. In our review, we highlight the different mechanisms of USP20 in various tumor types and demonstrate that USP20 regulates the stability of multiple proteins. Therefore, regulating the activity of USP20 is a novel tumor treatment. However, the clinical significance of USP20 in cancer treatment merits more evidence. Finally, different prospects exist for the continued research focus of USP20.

• Authors: Qiong Li, Chanqi Ye, Tian Tian, Qi Jiang, Peng Zhao, Xiaoting Wang, Feiye Liu, Jianzhen Shan, Jian Ruan
• Journal: Cell death & disease (Cell Death Dis) Vol. 13 Issue 5 Pg. 434 (05 04 2022) ISSN: 2041-4889 [Electronic] England
• PMID: 35508480 (Publication Type: Journal Article, Review, Research Support, Non-U.S. Gov't)
• Copyright: © 2022. The Author(s).

Chemical References

• USP20 protein, human
• Ubiquitin Thiolesterase
• Ubiquitin-Specific Proteases

Topics

• Breast Neoplasms
• Cell Transformation, Neoplastic
• Female
• Humans
• Ubiquitin Thiolesterase (genetics, metabolism)
• Ubiquitin-Specific Proteases (genetics, metabolism)
• Ubiquitination