Abstract
Non-small cell lung cancer (NSCLC) is the most common subtype of lung cancer. Ubiquitination is closely related to the development of lung cancer. However, the biological importance of newly discovered ubiquitin-specific peptidase (USP) 52 (USP52) in NSCLC remained unclear. Here, our findings identify USP52 as a novel tumor suppressor of NSCLC, the low expression of USP52 predicts a poor prognosis for NSCLC patients. The present study demonstrates that USP52 inhibits cancer cell proliferation through down-regulation of cyclin D1 (CCND1) as well as AKT/mTOR signaling pathway inhibition. Meanwhile, USP25 also suppresses NSCLC progression via enhancing phosphatase and tensin homolog (PTEN) stability in cancer cells, which further indicates the significance/importance of USP52 in NSCLC suppression.
Highlights
Lung cancer is a leading cause of cancer-related deaths worldwide
We discovered that USP52 plays an important role in Non-small cell lung cancer (NSCLC) suppression by inhibiting cancer cell proliferation via phosphatase and tensin homolog (PTEN) stabilization, which further indicated that USP52 plays an important role in NSCLC suppression
We examined the mRNA expression of USP52 in ten pairs of fresh primary NSCLC tissues compared with individual normal paracancerous tissues
Summary
Lung cancer is a leading cause of cancer-related deaths worldwide. Non-small cell lung cancer (NSCLC) is the most frequent subtype of lung cancer [1]. The understanding of genetic alterations that drive NSCLC is evolving. The ubiquitin system regulates essential cellular processes in eukaryotes. Ubiquitination directs the fate of many substrates, including proteasome degradation. The deubiquitinases drive the process of ubiquitin cleavage from substrates [4]. This process controls the stability of most cellular proteins, and its abnormal regulation leads to the occurrence of various human diseases, including cancer. Deubiquitinase inhibition can induce the degradation of selected proteins, which potentially includes some otherwise undruggable targets. The inhibition of ubiquitin-specific protease (USP) 7 (USP7) results in the degradation of the oncogenic E3 ligase MDM2 and the reactivation of the tumor suppressor p53 in various cancers [5]
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