The University of Southampton
University of Southampton Institutional Repository

The USP7 protein interaction network and its roles in tumorigenesis

The USP7 protein interaction network and its roles in tumorigenesis
The USP7 protein interaction network and its roles in tumorigenesis

Ubiquitin-specific protease (USP7), also known as Herpesvirus-associated ubiquitin-specific protease (HAUSP), is a deubiquitinase. There has been significant recent attention on USP7 following the discovery that USP7 is a key regulator of the p53-MDM2 pathway. The USP7 protein is 130 kDa in size and has multiple domains which bind to a diverse set of proteins. These interactions mediate key developmental and homeostatic processes including the cell cycle, immune response, and modulation of transcription factor and epigenetic regulator activity and localization. USP7 also promotes carcinogenesis through aberrant activation of the Wnt signalling pathway and stabilization of HIF-1α. These findings have shown that USP7 may induce tumour progression and be a therapeutic target. Together with interest in developing USP7 as a target, several studies have defined new protein interactions and the regulatory networks within which USP7 functions. In this review, we focus on the protein interactions of USP7 that are most important for its cancer-associated roles.

Cancer, Deubiquitinase, Protein network, Protein–protein interaction, Proteomics, USP7
Al-Eidan, Ahood
556ad339-b121-42e1-b873-ac99f905c774
Wang, Yihua
f5044a95-60a7-42d2-87d6-5f1f789e3a7e
Skipp, Paul
1ba7dcf6-9fe7-4b5c-a9d0-e32ed7f42aa5
Ewing, Rob M.
022c5b04-da20-4e55-8088-44d0dc9935ae
Al-Eidan, Ahood
556ad339-b121-42e1-b873-ac99f905c774
Wang, Yihua
f5044a95-60a7-42d2-87d6-5f1f789e3a7e
Skipp, Paul
1ba7dcf6-9fe7-4b5c-a9d0-e32ed7f42aa5
Ewing, Rob M.
022c5b04-da20-4e55-8088-44d0dc9935ae

Al-Eidan, Ahood, Wang, Yihua, Skipp, Paul and Ewing, Rob M. (2020) The USP7 protein interaction network and its roles in tumorigenesis. Genes and Diseases. (doi:10.1016/j.gendis.2020.10.004).

Record type: Review

Abstract

Ubiquitin-specific protease (USP7), also known as Herpesvirus-associated ubiquitin-specific protease (HAUSP), is a deubiquitinase. There has been significant recent attention on USP7 following the discovery that USP7 is a key regulator of the p53-MDM2 pathway. The USP7 protein is 130 kDa in size and has multiple domains which bind to a diverse set of proteins. These interactions mediate key developmental and homeostatic processes including the cell cycle, immune response, and modulation of transcription factor and epigenetic regulator activity and localization. USP7 also promotes carcinogenesis through aberrant activation of the Wnt signalling pathway and stabilization of HIF-1α. These findings have shown that USP7 may induce tumour progression and be a therapeutic target. Together with interest in developing USP7 as a target, several studies have defined new protein interactions and the regulatory networks within which USP7 functions. In this review, we focus on the protein interactions of USP7 that are most important for its cancer-associated roles.

Text
The USP7 protein - Version of Record
Download (804kB)

More information

Accepted/In Press date: 15 October 2020
e-pub ahead of print date: 22 October 2020
Keywords: Cancer, Deubiquitinase, Protein network, Protein–protein interaction, Proteomics, USP7

Identifiers

Local EPrints ID: 446512
URI: http://eprints.soton.ac.uk/id/eprint/446512
PURE UUID: e3e483f7-1107-48a2-b6fb-a55cc13682cc
ORCID for Yihua Wang: ORCID iD orcid.org/0000-0001-5561-0648
ORCID for Paul Skipp: ORCID iD orcid.org/0000-0002-2995-2959
ORCID for Rob M. Ewing: ORCID iD orcid.org/0000-0001-6510-4001

Catalogue record

Date deposited: 12 Feb 2021 17:30
Last modified: 18 Feb 2021 17:25

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×