USP14 Inhibition Regulates Tumorigenesis by Inducing Autophagy in Lung Cancer In Vitro release_ti5bry5gibb4reg3ka52x5c2ii

by Kyung Ho Han, Minseok Kwak, Tae Hyeong Lee, Min-soo Park, In-ho Jeong, Min Ji Kim, Jun-O Jin, Peter Lee

Published in International Journal of Molecular Sciences by MDPI AG.

2019   Volume 20, Issue 21, p5300


The ubiquitin–proteasome system is an essential regulator of several cellular pathways involving oncogenes. Deubiquitination negatively regulates target proteins or substrates linked to both hereditary and sporadic forms of cancer. The deubiquitinating enzyme ubiquitin-specific protease 14 (USP14) is associated with proteasomes where it trims the ubiquitin chain on the substrate. Here, we found that USP14 is highly expressed in patients with lung cancer. We also demonstrated that USP14 inhibitors (IU1-47 and siRNA-USP14) significantly decreased cell proliferation, migration, and invasion in lung cancer. Remarkably, we found that USP14 negatively regulates lung tumorigenesis not only through apoptosis but also through the autophagy pathway. Our findings suggest that USP14 plays a crucial role in lung tumorigenesis and that USP14 inhibitors are potent drugs in lung cancer treatment.
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Date   2019-10-24
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