Perspective abstract
Nature Chemical Biology 3, 697 - 705 (2007)
Published online: 18 October 2007 | doi:10.1038/nchembio.2007.43
Mechanisms, biology and inhibitors of deubiquitinating enzymes
Kerry Routenberg Love1, André Catic2, Christian Schlieker1 & Hidde L Ploegh1
Abstract
The addition of ubiquitin (Ub) and ubiquitin-like (Ubl) modifiers to proteins serves to modulate function and is a key step in protein degradation, epigenetic modification and intracellular localization. Deubiquitinating enzymes and Ubl-specific proteases, the proteins responsible for the removal of Ub and Ubls, act as an additional level of control over the ubiquitin-proteasome system. Their conservation and widespread occurrence in eukaryotes, prokaryotes and viruses shows that these proteases constitute an essential class of enzymes. Here, we discuss how chemical tools, including activity-based probes and suicide inhibitors, have enabled (i) discovery of deubiquitinating enzymes, (ii) their functional profiling, crystallographic characterization and mechanistic classification and (iii) development of molecules for therapeutic purposes.
- Kerry Routenberg Love, Christian Schlieker and Hidde L. Ploegh are at the Whitehead Institute for Biomedical Research, 9 Cambridge Center, Cambridge, Massachusetts 02142, USA.
- André Catic is at the Harvard Stem Cell Institute, Massachusetts General Hospital, 185 Cambridge Street, Boston, Massachusetts 02114, USA. e-mail: ploegh@wi.mit.edu
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