USP7: Structure, substrate specificity, and inhibition

Alexandra Pozhidaeva; Irina Bezsonova

doi:10.1016/j.dnarep.2019.02.005

USP7: Structure, substrate specificity, and inhibition

DNA Repair (Amst). 2019 Apr:76:30-39. doi: 10.1016/j.dnarep.2019.02.005. Epub 2019 Feb 16.

Authors

Alexandra Pozhidaeva¹, Irina Bezsonova²

Affiliations

¹ Department of Molecular Biology and Biophysics, UCONN Health, Farmington, CT, USA; Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
² Department of Molecular Biology and Biophysics, UCONN Health, Farmington, CT, USA. Electronic address: [email protected].

Abstract

Turnover of cellular proteins is regulated by Ubiquitin Proteasome System (UPS). Components of this pathway, including the proteasome, ubiquitinating enzymes and deubiquitinating enzymes, are highly specialized and tightly regulated. In this mini-review we focus on the de-ubiquitinating enzyme USP7, and summarize latest advances in understanding its structure, substrate specificity and relevance to human cancers. There is increasing interest in UPS components as targets for cancer therapy and here we also overview the recent progress in the development of small molecule inhibitors that target USP7.

Keywords: Cancer; DUB inhibition; Deubiquitinating enzyme; USP7; Ubiquitin-proteasome pathway.

Publication types

Review

MeSH terms

Animals
Enzyme Inhibitors / pharmacology*
Humans
Substrate Specificity
Ubiquitin-Specific Peptidase 7 / antagonists & inhibitors
Ubiquitin-Specific Peptidase 7 / chemistry*
Ubiquitin-Specific Peptidase 7 / metabolism*

Substances

Enzyme Inhibitors
Ubiquitin-Specific Peptidase 7

Grants and funding

R35 GM128864/GM/NIGMS NIH HHS/United States