Deubiquitinating c-Myc: USP36 steps up in the nucleolus

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24 Scopus citations


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 languageEnglish (US)
Pages (from-to)3786-3793
Number of pages8
JournalCell Cycle
Issue number24
StatePublished - Jan 1 2015


  • C-Myc
  • Deubiquitinating enzymes
  • Nucleolus
  • USP36
  • Ubiquitination

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology


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