Open AccessDeubiquitylation and stabilization of ARMC5 by ubiquitin‐specific processing protease 7 (USP7) are critical for RCC proliferation
Author(s) -
Yan Guobei,
Liu Na,
Tian Jun,
Fu Yanli,
Wei Wei,
Zou Jingjing,
Li Suping,
Wang Qing,
Li Kai,
Wang Junhua
Publication year - 2021
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/jcmm.16306
Subject(s) - deubiquitinating enzyme , ubiquitin , cell growth , gene knockdown , cancer research , chemistry , carcinogenesis , ubiquitin ligase , biology , microbiology and biotechnology , biochemistry , apoptosis , gene
The ubiquitin‐proteasome system is an essential regulator of ARMC5, which serves as a new tumour suppressor protein for inhibiting meningiomas and hereditary adrenocortical tumorigenesis. However, the precise mechanism for the deubiquitination of ARMC5 is still not fully understood. A Western blot analysis of ARMC5 was performed and showed that the expression of ARMC5 was decreased in the renal cancer cell tissues and lines. By screening a deubiquitinase library, we identified USP7 as a potential ARMC5 associated deubiquitinase. In this paper, we demonstrated that there was an interaction between USP7 and ARMC5 in vivo and in vitro. Employing the overexpression and knockdown assay indicated that USP7 could greatly increase the steady state of ARMC5 through the ubiquitin‐proteasome pathway and regulate ARMC5 ubiquitination. Moreover, USP7 altered cell cycle G1/S phases and regulated renal cancer cell proliferation by targeting ARMC5. Together, these results suggest that USP7 plays an important role in the RCC proliferation through modulating ARMC5 stability.