E3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53
- Authors
- Jung, J. H.; Bae, S.; Lee, J. Y.; Woo, S. R.; Cha, H. J.; Yoon, Y.; Suh, K-S; Lee, S-J; Park, I-C; Jin, Y-W; Lee, K-H; An, S.; Lee, J. H.
- Issue Date
- Dec-2011
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- p53; ubiquitination; E3 ligase
- Citation
- CELL DEATH AND DIFFERENTIATION, v.18, no.12, pp.1865 - 1875
- Indexed
- SCIE
SCOPUS
- Journal Title
- CELL DEATH AND DIFFERENTIATION
- Volume
- 18
- Number
- 12
- Start Page
- 1865
- End Page
- 1875
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/27645
- DOI
- 10.1038/cdd.2011.57
- ISSN
- 1350-9047
- 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. Cell Death and Differentiation (2011) 18, 1865-1875; doi:10.1038/cdd.2011.57; published online 20 May 2011
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