USP18 – a multifunctional component in the interferon response | Zendy

Anja Basters | Zendy; KlausPeter Knobeloch | Zendy; G. Fritz | Zendy

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USP18 – a multifunctional component in the interferon response

Author(s) -

Anja Basters,

KlausPeter Knobeloch,

G. Fritz

Publication year - 2018

Publication title -

bioscience reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.938

H-Index - 77

eISSN - 1573-4935

pISSN - 0144-8463

DOI - 10.1042/bsr20180250

Subject(s) - deubiquitinating enzyme , isg15 , proteases , ubiquitin , protease , interferon , gene , regulator , cleave , biology , ubiquitin conjugating enzyme , chemistry , enzyme , biochemistry , genetics , ubiquitin ligase

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.

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