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- W1993939968 abstract "Upon a certain DNA damage including cisplatin treatment, p73 is stabilized and exerts its growth-suppressive and/or proapoptotic function. However, the precise molecular basis by which the intracellular levels of p73 are regulated remains unclear. In the present study, we have identified RanBPM as a novel binding partner of p73α by yeast-based two-hybrid screening, and also found that RanBPM has an ability to stabilize p73α. GST pull-down assays and co-immunoprecipitation experiments revealed that RanBPM directly bound to the extreme COOH-terminal region of p73α, whereas it failed to interact with p53. Co-expression of RanBPM with p73α resulted in the nuclear translocation of RanBPM, and both proteins co-localized in cell nucleus as examined by indirect immunofluorescent staining. It is worth noting that the expression of RanBPM inhibited the ubiquitination of p73α, and thereby prolonged its half-life. Subsequent studies demonstrated that the proapoptotic activity of p73α was significantly enhanced in the presence of RanBPM. Taken together, our present findings implicate a novel role for RanBPM in the regulation of p73 stability and function." @default.
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- W1993939968 date "2004-11-22" @default.
- W1993939968 modified "2023-10-10" @default.
- W1993939968 title "Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells" @default.
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- W1993939968 doi "https://doi.org/10.1038/sj.onc.1208257" @default.
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