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Open AccessArticle

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

1
Department of Biomedical Sciences, University of Ulsan College of Medicine, Asan Medical Center, Seoul 05505, Korea
2
Department of Chemistry, Pukyong National University, Busan 48513, Korea
3
Department of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Korea
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2019, 20(21), 5300; https://doi.org/10.3390/ijms20215300
Received: 5 September 2019 / Revised: 16 October 2019 / Accepted: 23 October 2019 / Published: 24 October 2019
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. View Full-Text
Keywords: ubiquitin-specific protease 14; deubiquitinating enzyme; lung cancer; autophagy ubiquitin-specific protease 14; deubiquitinating enzyme; lung cancer; autophagy
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Han, K.H.; Kwak, M.; Lee, T.H.; Park, M.-S.; Jeong, I.-H.; Kim, M.J.; Jin, J.-O.; Lee, P. .-W. USP14 Inhibition Regulates Tumorigenesis by Inducing Autophagy in Lung Cancer In Vitro. Int. J. Mol. Sci. 2019, 20, 5300.

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