The deubiquitinating enzyme USP17 regulates c-Myc levels and controls cell proliferation and glycolysis

FEBS Letters

article

Mai Nagasaka¹  Yasumichi Inoue¹  Manaka Yoshida¹  Chiharu Miyajima¹  Daisuke Morishita¹  Muneshige Tokugawa¹  Haruna Nakamoto¹  Mayumi Sugano¹  Nobumichi Ohoka⁴  Hidetoshi Hayashi¹ 

[1] Department of Cell Signaling, Graduate School of Pharmaceutical Sciences, Nagoya City University;Department of Innovative Therapeutics Sciences, Cooperative Major in Nanopharmaceutical Sciences, Graduate School of Pharmaceutical Sciences, Nagoya City University;Chordia Therapeutics Inc.;Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences

关键词: c-Myc;    deubiquitination;    glycolysis;    proliferation;    USP17;   

DOI  :  10.1002/1873-3468.14296

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 upregulated expression of c-Myc in human cancers. We 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.

【 授权许可】

Unknown