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Targeting ubiquitin specific proteases for drug discovery

Daviet, Laurent, Colland, Frédéric·2008·Biochimie
DOI 10.1016/j.biochi.2007.09.013
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Abstract

Deregulation of the ubiquitin-proteasome system has been implicated in the pathogenesis of many human diseases, including cancer, neurodegenerative disorders and viral diseases. The recent approval of the proteasome inhibitor bortezomib (Velcade) for the treatment of multiple myeloma and mantle cell lymphoma establishes this system as a valid target for cancer treatment. A promising alternative to targeting the proteasome itself would be to interact at the level of the upstream, ubiquitin conjugation/deconjugation system to generate more specific, less toxic anticancer agents. Ubiquitin specific proteases (USP) are de-ubiquitinating enzymes which remove ubiquitin from specific protein substrates and allow protein salvage from proteasome degradation, regulation of protein localization or activation. Due to their protease activity and their involvement in several pathologies, USPs are emerging as potential target sites for pharmacological interference in the ubiquitin regulatory machinery. We will review here this class of enzymes from target validation to small molecule drug discovery.

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  • E3 ubiquitin ligases can be regulated by multiple DUBs.

    “Moreover, as E3s can be regulated by multiple DUBs (Daviet & Colland, 2008;Nathan et al, 2008), we used an unbiased siRNA-based approach to ask whether deubiquitination of parkin regulates its function in mitophagy.”

    From USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin (2014) · cites this paper as Daviet & Colland, 2008

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Metadata

Authors
Daviet, L., & Colland, F.
Venue
Biochimie
Publisher
Elsevier BV
Published
2008-02
Volume
90
Issue
2
Pages
270-283
ISSN
0300-9084
DOI
10.1016/j.biochi.2007.09.013
Cited by
126
References
11
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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