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the RNF20/40 complex, a major ubiquitin ligase catalysing histone H2B monoubiquitination, interacts with the motor protein Eg5 during mitosis and participates in spindle assembly.
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data indicate that RNF20 and PARP1 are synthetic lethal interactors
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RNF20 depletion stabilizes the ZSCAN4 protein half-life, suggesting that RNF20 negatively regulates ZSCAN4 stability.
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The effects of RNF20 on mammary tumorigenesis are subtype dependent: In basal-like cancers cells, RNF20 suppresses the NF-kappaB-dependent expression of cytokines, known to contribute to the growth of this tumor subtype.
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The authors also show that the RING domains of RNF20 and RNF40 can form a stable heterodimer that is active.
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Manipulation of key H2Bub1 E3 ubiquitin ligases, RNF20, RNF40 and BRCA1, in ovarian cancer cell line models modulated H2Bub1 levels, indicative of the role of these RING finger ligases in monoubiquitination of H2Bub1 in vitro
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RNF20 and H2Bub1 promotes chronic colonic inflammation and inflammation-associated colorectal cancer in mice and humans, partly by augmenting NF-kappaB activity and attenuating the antitumoral T cell response.
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It was observed that RE-IIBP induces MEIS1-mediated apoptosis, which was dependent on H2BK120 ubiquitination by RNF20.
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A primary role for FACT in RNF20 recruitment chromatin remodeling for initiation of homologous recombination repair.
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Together, these results indicate that human adenovirus E1A uses hBre1 to recruit the hPaf1 complex in order to optimally activate viral early transcription by enhancing transcriptional elongation.
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The ability of E1A to target hBre1 to simultaneously repress cellular IFN dependent transcription while activating viral transcription
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model whereby cotranscriptional recruitment of Rnf20 at MLL-fusion target genes leads to amplification of Dot1l-mediated H3K79 methylation, thereby rendering leukemia cells dependent on Rnf20 to maintain their oncogenic transcriptional program
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We show that Bre1 (human BRE1A/B (RNF20/40) and mouse Bre1a/b (Rnf20/40)) acts as an important suppressor of chromosomal instability
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our results suggest that RNF20 and RNF40, either via ubiquitylation of H2B or other targets, are coupled to the proliferation of prostate cancer cells.
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Studies indicate that H2B monoubiquitylation is driven primarily by an E3 ubiquitin ligase composed of the two RING finger proteins RNF20 and RNF40.
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RNF20, presumably via H2Bub, selectively represses oncogenic genes by interfering with chromatin recruitment of TFIIS, a factor capable of relieving stalled RNA polymerase II. RNF20 inhibits the interaction between TFIIS and the PAF1 complex.
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RNF20-mediated H2B ubiquitination at DSBs plays a critical role in HRR through chromatin remodeling
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the observed defects in the radiation response of Bre1a/b-deficient cells
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RNF20 overexpression leads to elevated histone 2B monoubiquitination, subsequently higher levels of methylation at H3 lysines 4 and 79, and stimulation of homeobox gene expression.
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The Bre1 protein specifically increases the global level of H2B ubiquitylation at lysine 120 and enhances activator-dependent transcription.