期刊
JOURNAL OF MOLECULAR CELL BIOLOGY
卷 9, 期 1, 页码 45-52出版社
OXFORD UNIV PRESS
DOI: 10.1093/jmcb/mjw049
关键词
HAUSP; USP7; p53 stability; MDM2 stability; HAUSP inhibitors; cancer
类别
资金
- National Cancer Institute, US National Institutes of Health (NIH) [5R01CA193890, 5RO1CA190477, 5RO1CA085533, 2P01CA080058]
- NIH Cancer Biology Training Grant [T32-CA09503]
It is well established that both p53 and MDM2 are short-lived proteins whose stabilities are tightly controlled through ubiquitination-mediated degradation. Although numerous studies indicate that the MDM2 E3 ligase activity, as well as the protein-protein interaction between p53 and MDM2, is the major focus for this regulation, emerging evidence suggests that the deubiquitinase herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) plays a critical role. Furthermore, HAUSP inhibition elevates p53 stability and might be beneficial for therapeutic purposes. In this review, we discuss the advances of this dynamic pathway and the contributions of positive and negative regulators affecting HAUSP activity. We also highlight the roles of HAUSP in cancer justifying the production of the first generation of HAUSP inhibitors.
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