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RNF126 Quenches RNF168 Function in the DNA Damage Response

Authors :
Zhang, Lianzhong
Wang, Zhenzhen
Shi, Ruifeng
Zhu, Xuefei
Zhou, Jiahui
Peng, Bin
Xu, Xingzhi
Source :
Genomics, Proteomics and Bioinformatics; December 2018, Vol. 16 Issue: 6 p428-438, 11p
Publication Year :
2018

Abstract

DNA damage response(DDR) is essential for maintaining genome stability and protecting cells from tumorigenesis. Ubiquitin and ubiquitin-like modifications play an important role in DDR, from signaling DNA damage to mediating DNA repair. In this report, we found that the E3 ligase ring finger protein 126 (RNF126) was recruited to UV laser micro-irradiation-induced stripes in a RNF8-dependent manner. RNF126 directly interacted with and ubiquitinated another E3 ligase, RNF168. Overexpression of wild type RNF126, but not catalytically-inactive mutant RNF126 (CC229/232AA), diminished ubiquitinationof H2A histone family member X (H2AX), and subsequent bleomycin-induced focus formation of total ubiquitin FK2, TP53-binding protein 1 (53BP1), and receptor-associated protein 80 (RAP80). Interestingly, both RNF126 overexpression and RNF126 downregulation compromised homologous recombination (HR)-mediated repair of DNA double-strand breaks (DSBs). Taken together, our findings demonstrate that RNF126 negatively regulates RNF168 function in DDR and its appropriate cellular expression levels are essential for HR-mediated DSB repair.

Details

Language :
English
ISSN :
16720229
Volume :
16
Issue :
6
Database :
Supplemental Index
Journal :
Genomics, Proteomics and Bioinformatics
Publication Type :
Periodical
Accession number :
ejs66359170
Full Text :
https://doi.org/10.1016/j.gpb.2018.07.004