Abstract
Abstract The ubiquitin proteasome system (UPS) is the primary pathway through which the levels of regulatory proteins are controlled. Dysregulation of components within the UPS have been linked to both hereditary and sporadic forms of cancer. The deubiquitinating enzyme USP14 is associated with proteasome where it is trimming ubiquitin chain on the substrate. In our current study, we unexpectedly found that USP14 levels were elevated in lung cancer patients. USP14 inhibitor, IU1-47 and siUSP14, significantly decreased cell proliferation, migration, and invasiveness in lung cancer cells. Inhibition of USP14 induced the alteration of LC3-I to LC3-II which leads to autophagic cell death not but apoptosis. Thus our finding suggests that USP14 plays a crucial role in tumorigenesis and USP 14 inhibitor is a potent drug for lung cancer treatment. Citation Format: MINSOO PARK, Min Ji Kim, Peter Chang Whan Lee. Inhibition of USP14 decrease tumorigenesis via autophagy in lung cancer [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2019; 2019 Mar 29-Apr 3; Atlanta, GA. Philadelphia (PA): AACR; Cancer Res 2019;79(13 Suppl):Abstract nr 4276.
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