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E3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53

Title
E3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53
Author
이수재
Keywords
Tumour-suppressor proteins; Ubiquitin ligases; Ubiquitylation
Issue Date
2011-12
Publisher
Nature Publishing Group
Citation
CELL DEATH AND DIFFERENTIATION, 2011, 18(12), P.1865-1875
Abstract
Following DNA damage, p53 translocates to the cytoplasm and mitochondria, where it triggers transcription-independent apoptosis by binding to Bcl-2 family proteins. However, little is known about how this exonuclear function of p53 is regulated. Here, we identify and characterize a p53-interacting protein called Hades, an E3 ligase that interacts with p53 in the mitochondria. Hades reduces p53 stability via a mechanism that requires its RING-finger domain with ubiquitin ligase activity. Hades polyubiquitinates p53 in vitro independent of Mdm2 and targets a critical lysine residue in p53 (lysine 24) distinct from those targeted by Mdm2. Hades inhibits a p53-dependent mitochondrial cell death pathway by inhibiting p53 and Bcl-2 interactions. These findings show that Hades-mediated p53 ubiquitination is a novel mechanism for negatively regulating the exonuclear function of p53.
URI
https://www.nature.com/articles/cdd201157http://hdl.handle.net/20.500.11754/65910
ISSN
1350-9047
DOI
10.1038/cdd.2011.57
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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