The c-Myc oncoprotein is frequently overexpressed in human cancers and is essential for cancer cell proliferation. The dysregulation of ubiquitin-proteasome-mediated degradation is one of the contributing factors to the up-regulated expression of c-Myc in human cancers.
In the present study, Dr. Hidetoshi Hayashi (Professor, Nagoya City University) and collaborators herein identified USP17 as a novel deubiquitinating enzyme that regulates c-Myc levels and controls cell proliferation and glycolysis. The overexpression of USP17 stabilized the c-Myc protein by promoting its deubiquitination. In contrast, the knockdown of USP17 promoted c-Myc degradation and reduced c-Myc levels. The knockdown of USP17 also suppressed cell proliferation and glycolysis. Collectively, the present results reveal a novel role for USP17 in the regulation of c-Myc stability, and suggest its potential as a therapeutic target for cancer treatment.
FEBS Letters
Experimental study
Cells
The deubiquitinating enzyme USP17 regulates c-Myc levels and controls cell proliferation and glycolysis
28-Feb-2022