6-Thioguanine is a noncompetitive and slow binding inhibitor of human deubiquitinating protease USP2 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Shang-Ju Chuang, Shu-Chun Cheng, Hui-Chi Tang, Chiao-Yin Sun, Chi-Yuan Chou

ABSTRACT

Ubiquitin-specific protease 2 (USP2) belongs to the family of deubiquitinases that can rescue protein targets from proteasomal degradation by reversing their ubiquitination. In various cancers, including prostate cancer and ovarian carcinoma, upregulation of USP2 leads to an increase in the levels of deubiquitinated substrates such as fatty acid synthase, MDM2, cyclin D1 and Aurora-A. USP2 thus plays a critical role in tumor cells' survival and therefore represents a therapeutic target. Here a leukemia drug, 6-thioguanine, was found to be a potent inhibitor of USP2. Enzyme-kinetic and X-ray crystallographic data suggest that 6-thioguanine displays a noncompetitive and slow-binding inhibitory mechanism against USP2. Our study provides a clear rationale for the clinical evaluation of 6-thioguanine for USP2-upregulated cancers. More... »

PAGES

3102

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-21476-w

DOI

http://dx.doi.org/10.1038/s41598-018-21476-w

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1100951804

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29449607


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