RNF125 is a Ubiquitin-Protein Ligase that Promotes p53 Degradation
| العنوان: | RNF125 is a Ubiquitin-Protein Ligase that Promotes p53 Degradation |
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| المؤلفون: | Bing Zhou, Xiaoqing Huo, Xiaorui Li, Zhanhui Miao, Weiwei Li, Zhihong Lu, Yang Liuzhong |
| المصدر: | Cellular Physiology and Biochemistry, Vol 35, Iss 1, Pp 237-245 (2015) |
| بيانات النشر: | Cell Physiol Biochem Press GmbH & Co KG, 2015. |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | Transcriptional Activation, p53, Proteasome Endopeptidase Complex, RNF125, Leupeptins, Physiology, Ubiquitin-Protein Ligases, Down-Regulation, Transfection, lcsh:Physiology, lcsh:Biochemistry, Proteasome degradation, Humans, Immunoprecipitation, lcsh:QD415-436, RNA, Small Interfering, Cell Proliferation, biology, lcsh:QP1-981, Chemistry, Ubiquitination, P53 Tumor Suppressor, HCT116 Cells, Cell biology, Ubiquitin ligase, HEK293 Cells, Amino Acid Substitution, E3 ubiquitin ligase, Proteolysis, biology.protein, Mdm2, Degradation (geology), RNA Interference, Tumor Suppressor Protein p53, Protein Binding |
| الوصف: | Background/Aims: Although early studies show that Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. Here, we investigated the role of RNF125, a non-Mdm2 ubiquitin-protein ligase, in the regulation of p53. Methods and Results: RNF125 physically interacted with p53 in exogenous/endogenous co-immunoprecipitation (IP) and GST-pull down assay, and a C72/75A mutation of RNF125 did not interfere with this interaction. Expression of RNF125 decreased the level of p53 in a dose-dependent manner, whereas knockdown of RNF125 by RNA interference increased the level of p53. As shown by Western blotting and ubiquitin assay, RNF125 ubiquitinated p53 and targeted it for proteasome degradation. Furthermore, RNF125 repressed p53 functions including p53-dependent transactivation and growth inhibition. Conclusion: Our data suggest that RNF125 negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. |
| اللغة: | English |
| تدمد: | 1421-9778 1015-8987 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4edc3b648c8d18636e83891e801ed2c http://www.karger.com/Article/FullText/369691 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....f4edc3b648c8d18636e83891e801ed2c |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14219778 10158987 |
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