E3 ubiquitin ligase Hades negatively regulates the exonuclear function of p53 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-12

AUTHORS

J H Jung, S Bae, J Y Lee, S R Woo, H J Cha, Y Yoon, K-S Suh, S-J Lee, I-C Park, Y-W Jin, K-H Lee, S An, J H Lee

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. More... »

PAGES

1865

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/cdd.2011.57

DOI

http://dx.doi.org/10.1038/cdd.2011.57

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042038425

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21597459


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