期刊
BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON CANCER
卷 1855, 期 1, 页码 50-60出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbcan.2014.11.005
关键词
Cancer; SCF; Ubiquitin ligase; Deubiquitinating enzyme; Drug targets
资金
- NIH [GM089763, GM094777, CA177910]
- NSFC [81172087]
- Priority Academic Program Development of Jiangsu Higher Education Institutions
- NATIONAL CANCER INSTITUTE [R01CA177910] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM089763, R01GM094777] Funding Source: NIH RePORTER
Proteasome-mediated degradation is a common mechanism by which cells renew their intracellular proteins and maintain protein homeostasis. In this process, the E3 ubiquitin ligases are responsible for targeting specific substrates (proteins) for ubiquitin-mediated degradation. However, in cancer cells, the stability and the balance between oncoproteins and tumor suppressor proteins are disturbed in part due to deregulated proteasome-mediated degradation. This ultimately leads to either stabilization of oncoprotein(s) or increased degradation of tumor suppressor(s), contributing to tumorigenesis and cancer progression. Therefore, E3 ubiquitin ligases including the SCF types of ubiquitin ligases have recently evolved as promising therapeutic targets for the development of novel anti-cancer drugs. In this review, we highlighted the critical components along the ubiquitin pathway including El, E2, various E3 enzymes and DUBs that could serve as potential drug targets and also described the available bioactive compounds that target the ubiquitin pathway to control various cancers. (C) 2014 Elsevier B.V. All rights reserved.
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