USP18 – a multifunctional component in the interferon response
- Basters, Anja Friedrich Miescher Institute for Biomedical Research, Quantitative Biology, Basel, Switzerland
- Knobeloch, Klaus-Peter Faculty of Medicine, Institute of Neuropathology, University of Freiburg, Freiburg, Germany
- Fritz, Günter Institute of Microbiology, University of Hohenheim, Stuttgart, Germany
- 2018-11-16
Published in:
- Bioscience Reports. - Portland Press Ltd.. - 2018, vol. 38, no. 6
English
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.
- Language
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- English
- Open access status
- gold
- Identifiers
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- DOI 10.1042/bsr20180250
- ISSN 0144-8463
- Persistent URL
- https://folia.unifr.ch/global/documents/114511
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