Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain | Health & Environmental Research Online (HERO)

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Citation
Tags

HERO ID

4103791

Reference Type

Journal Article

Title

Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain

Author(s)

Luna-Vargas, MP; Faesen, AC; van Dijk, WJ; Rape, M; Fish, A; Sixma, TK

Year

2011

Is Peer Reviewed?

Yes

Journal

EMBO Reports
ISSN: 1469-221X

Volume

Issue

Page Numbers

365-372

Language

English

PMID

21415856

DOI

10.1038/embor.2011.33

Web of Science Id

WOS:000289073200017

Relationship(s)

has retraction 4101930 Retraction: '' by MP Luna-Vargas, AC Faesen, WJ van Dijk, M Rape, A Fish, TK Sixma

Abstract

USP4 is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes that has a role in spliceosome regulation. Here, we show that the crystal structure of the minimal catalytic domain of USP4 has the conserved USP-like fold with its typical ubiquitin-binding site. A ubiquitin-like (Ubl) domain inserted into the catalytic domain has autoregulatory function. This Ubl domain can bind to the catalytic domain and compete with the ubiquitin substrate, partially inhibiting USP4 activity against different substrates. Interestingly, other USPs, such as USP39, could relieve this inhibition.