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Review
. 2019 May 27;26(1):42.
doi: 10.1186/s12929-019-0522-0.

The role of ubiquitin-specific peptidases in cancer progression

Affiliations
Review

The role of ubiquitin-specific peptidases in cancer progression

Ming-Jer Young et al. J Biomed Sci. .

Abstract

Protein ubiquitination is an important mechanism for regulating the activity and levels of proteins under physiological conditions. Loss of regulation by protein ubiquitination leads to various diseases, such as cancer. Two types of enzymes, namely, E1/E2/E3 ligases and deubiquitinases, are responsible for controlling protein ubiquitination. The ubiquitin-specific peptidases (USPs) are the main members of the deubiquitinase family. Many studies have addressed the roles of USPs in various diseases. An increasing number of studies have indicated that USPs are critical for cancer progression, and some USPs have been used as targets to develop inhibitors for cancer prevention. Herein we collect and organize most of the recent studies on the roles of USPs in cancer progression and discuss the development of USP inhibitors for cancer therapy in the future.

Keywords: Cancer; Deubiquitinases; Ubiquitin-specific peptidases; Ubiquitination.

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Conflict of interest statement

The authors declare that they have no competing interests.

Figures

Fig. 1
Fig. 1
The USP family of proteins contain conserved and nonconserved catalytic regions. a Conservation score of the USP residue. The structure of USP7 (PDB ID: 5N9R) is used as a reference. Regions are shaded in blue, indicating nonconserved, or red, indicating conserved. The insert shows USP7 catalytic site residues and cocrystal ligand (yellow) as a stick model. The sequence pattern for the USP protein family is shown, with the USP7 sequence as a reference. Sites are highlighted as shown. The green line denotes the hydrogen bond. b Sequence alignment of Site 1 (green) and Site 2 (yellow). The sequence pattern figure was produced using the weblogo3 server (http://weblogo.threeplusone.com/create.cgi).

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