Journal
JOURNAL OF CELLULAR PHYSIOLOGY
Volume 232, Issue 12, Pages 3664-3676Publisher
WILEY
DOI: 10.1002/jcp.25841
Keywords
c-Myc; breast cancer; deubiquitination; DUB; proteolysis; USP22
Categories
Funding
- Yonsei University [2015-22-0055]
- Korea Health Industry Development Institute [HI14C0093]
- National Research Foundation of Korea [2014M3C7A1064545, 2015R1A2A2A01003080]
- National Research Foundation of Korea [2015R1A2A2A01003080, 2014M3C7A1064545] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The proto-oncogene c-Myc has a pivotal function in growth control, differentiation, and apoptosis and is frequently affected in human cancer, including breast cancer. Ubiquitin-specific protease 22 (USP22), a member of the USP family of deubiquitinating enzymes (DUBs), mediates deubiquitination of target proteins, including histone H2B and H2A, telomeric repeat binding factor 1, and cyclin B1. USP22 is also a component of the mammalian SAGA transcriptional co-activating complex. In this study, we explored the functional role of USP22 in modulating c-Myc stability and its physiological relevance in breast cancer progression. We found that USP22 promotes deubiquitination of c-Myc in several breast cancer cell lines, resulting in increased levels of c-Myc. Consistent with this, USP22 knockdown reduces c-Myc levels. Furthermore, overexpression of USP22 stimulates breast cancer cell growth and colony formation, and increases c-Myc tumorigenic activity. In conclusion, the present study reveals that USP22 in breast cancer cell lines increases c-Myc stability through c-Myc deubiquitination, which is closely correlated with breast cancer progression.
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