USP7 Substrates Identified by Proteomics Analysis Reveal the Specificity of USP7

Authors

Litong Nie
Chao Wang
Xiaoguang Liu
Hongqi Teng
Siting Li
Min Huang
Xu Feng
Guangsheng Pei
Qinglei Hang
Zhongming Zhao
Boyi Gan
Li Ma
Junjie Chen

Language

English

Publication Date

9-1-2022

Journal

Genes Development

DOI

10.1101/gad.349848.122

PMID

36302555

PMCID

PMC9732911

PubMedCentral® Posted Date

9-1-2022

PubMedCentral® Full Text Version

Post-print

Abstract

Deubiquitylating enzymes (DUBs) remove ubiquitin chains from proteins and regulate protein stability and function. USP7 is one of the most extensively studied DUBs, since USP7 has several well-known substrates important for cancer progression, such as MDM2, N-MYC, and PTEN. Thus, USP7 is a promising drug target. However, systematic identification of USP7 substrates has not yet been performed. In this study, we carried out proteome profiling with label-free quantification in control and single/double-KO cells of

Keywords

Ubiquitin-Specific Peptidase 7, Proteomics, Ubiquitin Thiolesterase, Proteome, Ubiquitin, Ubiquitination

Published Open-Access

yes

Recommended Citation

Nie, Litong; Wang, Chao; Liu, Xiaoguang; et al., "USP7 Substrates Identified by Proteomics Analysis Reveal the Specificity of USP7" (2022). Faculty, Staff and Student Publications. 580.
https://digitalcommons.library.tmc.edu/uthshis_docs/580