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A conserved RAD6-MDM2 ubiquitin ligase machinery targets histone chaperone ASF1A in tumorigenesis.

Oncotarget. 2015; 
Wang C,,, Chang JF,, Yan H, Wang DL, Liu Y, Jing Y, Zhang M, Men YL, Lu D, Yang XM, Chen S,,, Sun FL,.
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Peptide Synthesis … HL-7702 cells were transfected with Myc-RAD6 plasmids; non-transfected cells were used as a negative control. In the first immunoprecipitation step, anti-Myc was used to pull down RAD6, and the Myc peptide (GenScript) was used to elute the complex … Get A Quote

摘要

Chromatin is a highly organized and dynamic structure in eukaryotic cells. The change of chromatin structure is essential in many cellular processes, such as gene transcription, DNA damage repair and others. Anti-silencing function 1 (ASF1) is a histone chaperone that participates in chromatin higher-order organization and is required for appropriate chromatin assembly. In this study, we identified the E2 ubiquitin-conjugating enzyme RAD6 as an evolutionary conserved interacting protein of ASF1 in D. melanogaster and H. sapiens that promotes the turnover of ASF1A by cooperating with a well-known E3 ligase, MDM2, via ubiquitin-proteasome pathway in H. sapiens. Further functional analyses indicated that the inter... More

关键词

ASF1A; MDM2; RAD6; protein degradation; tumorigenesis