The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Huang J,Xu LG,Liu T,Zhai Z,Shu HB

doi

10.1016/j.febslet.2005.09.105

keywords:

subject

Has Abstract

pub_date

2006-02-06 00:00:00

pages

940-7

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00053-6

journal_volume

580

pub_type

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