RNF112 Facilitates Ubiquitin‐Mediated Degradation of c‐Myc, Suppressing Proliferation, Migration and Lipid Synthesis in Bladder Cancer

The E3 ubiquitin ligase RNF112 is significantly downregulated in bladder cancer (BLCA) and is correlated with disease progression. In vitro and in vivo studies indicated that RNF112 suppresses BLCA cell proliferation, migration, and lipid synthesis. Mechanistically, RNF112 directly interacts with the MB II domain of MYC through its N-terminal zinc finger motif, and its catalytic site C97 facilitates K48-linked polyubiquitination of the K389 residue on the c-Myc protein, accelerating its degradation. Additionally, this research validated the interaction of c-Myc with the promoter of ATP citrate lyase (ACLY), a central enzyme of lipid metabolism, promoting its transcriptional activity. The restoration of c-Myc or ACLY expression attenuated the inhibitory effects of RNF112 on BLCA cell growth, migration, and lipid synthesis. In conclusion, this study confirmed that RNF112 suppressed the proliferation, migration, and lipid synthesis of BLCA cells by facilitating the ubiquitin-mediated degradation of c-Myc.

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Publication Details

Journal
Advanced Science
Published
2025-04-03
DOI
https://doi.org/10.1002/advs.202408311
Citations
1
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
0.81

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article

RNF112 Facilitates Ubiquitin‐Mediated Degradation of c‐Myc, Suppressing Proliferation, Migration and Lipid Synthesis in Bladder Cancer

Kaiyu Qian, Hong Weng, Xinghuan Wang, Huimin Xu et al.
1 citations
Advanced Science
Ubiquitin and proteasome pathways
0.81
article

RNF112 Facilitates Ubiquitin‐Mediated Degradation of c‐Myc, Suppressing Proliferation, Migration and Lipid Synthesis in Bladder Cancer

Kaiyu Qian, Hong Weng, Xinghuan Wang, Huimin Xu, Jingtian Yu, Lingao Ju, Yejinpeng Wang, Yu Xiao, Sheng Tu, Gang Wang, Yi Zhang, Mingxing Li, Siming Chen, Kangping Xiong
article en
1 citations

Abstract

The E3 ubiquitin ligase RNF112 is significantly downregulated in bladder cancer (BLCA) and is correlated with disease progression. In vitro and in vivo studies indicated that RNF112 suppresses BLCA cell proliferation, migration, and lipid synthesis. Mechanistically, RNF112 directly interacts with the MB II domain of MYC through its N-terminal zinc finger motif, and its catalytic site C97 facilitates K48-linked polyubiquitination of the K389 residue on the c-Myc protein, accelerating its degradation. Additionally, this research validated the interaction of c-Myc with the promoter of ATP citrate lyase (ACLY), a central enzyme of lipid metabolism, promoting its transcriptional activity. The restoration of c-Myc or ACLY expression attenuated the inhibitory effects of RNF112 on BLCA cell growth, migration, and lipid synthesis. In conclusion, this study confirmed that RNF112 suppressed the proliferation, migration, and lipid synthesis of BLCA cells by facilitating the ubiquitin-mediated degradation of c-Myc.

Advanced ScienceVol. 12(20)
Peking University (CN), Sir Run Run Shaw Hospital (CN), Wuhan University (CN), Zhongnan Hospital of Wuhan University (CN), Wuhan Center for Disease Control and Prevention (CN), Euler Technology (China), Zhejiang University (CN)
National Natural Science Foundation of China
Openalex Percentile: Top 29%
Ubiquitin and proteasome pathways
0.81
DOIOpen Access PDFOpenAlex
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