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- W1996260588 abstract "Recently, it has been shown that really interesting new gene (RING)–in between ring finger (IBR)–RING domain-containing proteins, such as Parkin and Parc, are E3 ubiquitin ligases and are involved in regulation of apoptosis. In this report, we show that p53-inducible RING-finger protein (p53RFP), a p53-inducible E3 ubiquitin ligase, induces p53-dependent but caspase-independent apoptosis. p53RFP contains an N-terminal RING–IBR–RING domain and an uncharacterized, evolutionally highly conserved C-terminal domain. p53RFP interacts with E2 ubiquitin-conjugating enzymes UbcH7 and UbcH8 but not with UbcH5, and this interaction is mediated through the RING–IBR–RING domain of p53RFP. Interestingly, the conserved C-terminal domain of p53RFP is required and sufficient for p53RFP-mediated apoptosis, suggesting p53RFP-mediated apoptosis does not require its E3 ubiquitin ligase activity. Together with a recent report showing that p53RFP is involved in ubiquitination and degradation of p21, a p53 downstream protein promoting growth arrest and antagonizing apoptosis, our findings suggest that p53RFP is involved in switching a cell from p53-mediated growth arrest to apoptosis." @default.
- W1996260588 created "2016-06-24" @default.
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- W1996260588 date "2006-01-18" @default.
- W1996260588 modified "2023-09-23" @default.
- W1996260588 title "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis" @default.
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- W1996260588 doi "https://doi.org/10.1016/j.febslet.2005.09.105" @default.
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