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USP18 – a multifunctional component in the interferon response

Identifieur interne : 000683 ( Main/Exploration ); précédent : 000682; suivant : 000684

USP18 – a multifunctional component in the interferon response

Auteurs : Anja Basters [Suisse] ; Klaus-Peter Knobeloch [Allemagne] ; Günter Fritz [Allemagne]

Source :

RBID : PMC:6240716

Abstract

Ubiquitin-specific proteases (USPs) represent the largest family of deubiquitinating enzymes (DUB). These proteases cleave the isopeptide bond between ubiquitin and a lysine residue of a ubiquitin-modified protein. USP18 is a special member of the USP family as it only deconjugates the ubiquitin-like protein ISG15 (interferon-stimulated gene (ISG) 15) from target proteins but is not active towards ubiquitin. Independent of its protease activity, USP18 functions as a major negative regulator of the type I interferon response showing that USP18 is – at least – a bifunctional protein. In this review, we summarise our current knowledge of protease-dependent and -independent functions of USP18 and discuss the structural basis of its dual activity.


Url:
DOI: 10.1042/BSR20180250
PubMed: 30126853
PubMed Central: 6240716


Affiliations:


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<analytic>
<author>
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<author>
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<li>District de Stuttgart</li>
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