Open AccessThe regulation of NONO by USP11 via deubiquitination is linked to the proliferation of melanoma cells
Author(s) -
Feng Peifu,
Li Ling,
Dai Jing,
Zhou Lingli,
Liu Jing,
Zhao Jinfeng,
Li Xiaodong,
Ling Neng,
Qiu Siyuan,
Zhang Lin,
Xie Tiantian,
Chen Yinglei,
Donovan Michael J.,
Peng Tianhuan,
Song Jianhui,
Ye Mao
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.16243
Subject(s) - biology , deubiquitinating enzyme , cell growth , melanoma , microbiology and biotechnology , ubiquitin , cancer research , biochemistry , gene
Ubiquitin‐specific protease 11 (USP11) has been implicated in the regulation of DNA repair, apoptosis, signal transduction and cell cycle. It belongs to a USP subfamily of deubiquitinases. Although previous research has shown that USP11 overexpression is frequently found in melanoma and is correlated with a poor prognosis, the potential molecular mechanism of USP11 in melanoma remains indefinitive. Here, we report that USP11 and NONO colocalize and interact with each other in the nucleus of melanoma cells. As a result, the knockdown of USP11 decreases NONO levels. Whereas, overexpression of USP11 increases NONO levels in a dose‐dependent manner. Furthermore, we reveal that USP11 protects NONO protein from proteasome‐mediated degradation by removing poly‐ubiquitin chains conjugated onto NONO. Functionally, USP11 mediated melanoma cell proliferation via the regulation of NONO levels because ablation of USP11 inhibits the proliferation which could be rescued by ectopic expression of NONO protein. Moreover, a significant positive correlation between USP11 and NONO concentrations was found in clinical melanoma samples. Collectively, these results demonstrate that USP11 is a new deubiquitinase of NONO and that the signalling axis of USP11‐NONO is significantly involved in melanoma proliferation.