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Molecular Carcinogenesis

Molecular Carcinogenesis

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USP12 promotes nonsmall cell lung cancer progression through deubiquitinating and stabilizing RRM2.

Published:1 October 2023 DOI: 10.1002/mc.23593 PMID: 37341611
Congcong Chen, Ning Xue, Kangshou Liu, Qiang He, Cong Wang, Yanguan Guo, Jiaxin Tian, Xinjian Liu, Yunlong Pan, Guo Chen

Abstract

RRM2 is the catalytic subunit of ribonucleotide reductase (RNR), which catalyzes de novo synthesis of deoxyribonucleotide triphosphates (dNTPs) and plays critical roles in cancer cell proliferation. RRM2 protein level is controlled by ubiquitination mediated protein degradation system; however, its deubiquitinase has not been identified yet. Here we showed that ubiquitin-specific peptidase 12 (USP12) directly interacts with and deubiquitinates RRM2 in non-small cell lung cancer (NSCLC) cells. Knockdown of USP12 causes DNA replication stress and retards tumor growth in vivo and in vitro. Meanwhile, USP12 protein levels were positively correlated to RRM2 protein levels in human NSCLC tissues. In addition, high expression of USP12 was associated with poor prognosis in NSCLC patients. Therefore, our study reveals that USP12 is a RRM2 regulator and targeting USP12 could be considered as a potential therapeutical strategy for NSCLC treatment.

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