Current Cancer Drug Targets

Ruiwen Zhang 
Texas Tech University Health Sciences Center
1300 Coulter Drive
Amarillo, TX 79106


Deubiquitinating Enzyme Inhibitors and their Potential in Cancer Therapy

Author(s): Bernat Crosas

Affiliation: Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 4, 08028 Barcelona, Spain.

Keywords: Deubiquitinating enzymes, DUBs, inhibitors, proteasome, small-molecule, ubiquitin specific proteases, USP1, USP7, USP8, USP9x, USP14.

Graphical Abstract:


Deubiquitinating enzymes (or DUBs) attack the ubiquitin-based isopeptide bond, thus counteracting ubiquitinprotein ligase activity in vivo. By disassembling ubiquitin-substrate and ubiquitin-ubiquitin covalent links, deubiquitinating enzymes exert a very powerful control of many signaling processes within the ubiquitin-proteasome system (UPS). Very active research in this field in the last decade shows that deubiquitinating enzymes play important regulatory roles in aspects relevant to cancer, such as proteasome activity, p53 stability, the regulation of fanconi anemia related proteins, tumor cell apoptosis induction, to mention a few. Thus, deubiquitinating enzymes have emerged as interesting drug targets in cancer research. Here, the pharmacological inhibition of DUBs and its potential effect in cancer treatment are reviewed.

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Article Details

Page: [506 - 516]
Pages: 11
DOI: 10.2174/1568009614666140725090620