Abstract
Ubiquitination plays a key and complex role in the regulation of c-Myc stability, transactivation, and oncogenic activity. c-Myc is ubiquitinated by a number of ubiquitin ligases (E3s), such as SCFFbw7 and SCFSkp2. Depending on the E3s, ubiquitination can either positively or negatively regulate c-Myc levels and activity. Meanwhile, c-Myc ubiquiti-nation can be reversed by deubiquitina-tion. An early study showed that USP28 deubiquitinates c-Myc via interacting with Fbw7α whereas a recent study reveals that USP37 deubiquitinates c-Myc independently of Fbw7 and c-Myc phosphorylation. Consequently, both USP28 and USP37 stabilize c-Myc and enhance its activity. We recently found the nucleolar USP36 as a novel c-Myc deubiquitinase that controls the end-point of c-Myc degradation pathway in the nucleolus. Here we briefly review the current understanding of ubiquitination and deubiquitination regulation of c-Myc and further discuss the USP36-c-Myc regulatory pathway.
Original language | English (US) |
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Pages (from-to) | 3786-3793 |
Number of pages | 8 |
Journal | Cell Cycle |
Volume | 14 |
Issue number | 24 |
DOIs | |
State | Published - Jan 1 2015 |
Keywords
- C-Myc
- Deubiquitinating enzymes
- Nucleolus
- USP36
- Ubiquitination
ASJC Scopus subject areas
- Molecular Biology
- Developmental Biology
- Cell Biology