Journal
BIOSCIENCE REPORTS
Volume 38, Issue -, Pages -Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BSR20180250
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Funding
- Heisenberg Fellowship of the Deutsche Forschungsgemeinschaft [FR 1488/3-2]
- Deutsche Forschungsgemeinschaft [KN 590/5-1, ERA_NET BacVirISG15]
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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 amajor 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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