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RING finger protein 31 promotes p53 degradation in breast cancer cells
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2016 (English)In: Oncogene, ISSN 0950-9232, E-ISSN 1476-5594, Vol. 35, no 15, 1955-1964 p.Article in journal (Refereed) PublishedText
Abstract [en]

The atypical E3 ubiquitin ligase RNF31 is highly expressed in human breast cancer, the most frequent neoplastic lethality among women. Here, RNF31 depletion in breast cancer cells in combination with global gene expression profiling revealed p53 (TP53) signaling as a potential RNF31 target. Interestingly, RNF31 decreased p53 stability, whereas depletion of RNF31 in breast cancer cells caused cell cycle arrest and cisplatin-induced apoptosis in a p53-dependent manner. Furthermore, RNF31 associated with the p53/MDM2 complex and facilitated p53 polyubiquitination and degradation by stabilizing MDM2, suggesting a molecular mechanism by which RNF31 regulates cell death. Analysis of publically available clinical data sets displayed a negative correlation between RNF31 and p53 target genes, including IGFBP3 and BTG1, consistent with RNF31 regulating p53 function in vivo as well. Together, our findings suggest RNF31 as a potential therapeutic target to restore p53 function in breast cancer.

Place, publisher, year, edition, pages
Nature Publishing Group, 2016. Vol. 35, no 15, 1955-1964 p.
Keyword [en]
ESTROGEN-RECEPTOR-ALPHA, MDM2 ANTAGONIST NUTLIN-3, UBIQUITIN LIGASE ACTIVITY, TRANSCRIPTIONAL REPRESSION, GERMLINE POLYMORPHISMS, ONCOPROTEIN MDM2, APOPTOSIS, E3, ACTIVATION, MUTATIONS
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Cell and Molecular Biology
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URN: urn:nbn:se:kth:diva-186617DOI: 10.1038/onc.2015.260ISI: 000374010300008PubMedID: 26148235ScopusID: 2-s2.0-84935442275OAI: oai:DiVA.org:kth-186617DiVA: diva2:931961
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QC 20160531

Available from: 2016-05-31 Created: 2016-05-13 Last updated: 2016-05-31Bibliographically approved

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Williams, Cecilia
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Proteomics and NanobiotechnologyScience for Life Laboratory, SciLifeLab
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