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Oncogene. 2007 Jun 14;26(28):4059-70. Epub 2007 Jan 15.

Ubiquitin-independent degradation of p53 mediated by high-risk human papillomavirus protein E6.

Author information

1
Department of Cell Cycle Control, Institute of Molecular and Cell Biology, Proteos, Singapore. scamus@imcb.a-star.edu.sg

Abstract

In vitro, high-risk human papillomavirus E6 proteins have been shown, in conjunction with E6-associated protein (E6AP), to mediate ubiquitination of p53 and its degradation by the 26S proteasome by a pathway that is thought to be analogous to Mdm2-mediated p53 degradation. However, differences in the requirements of E6/E6AP and Mdm2 to promote the degradation of p53, both in vivo and in vitro, suggest that these two E3 ligases may promote p53 degradation by distinct pathways. Using tools that disrupt ubiquitination and degradation, clear differences between E6- and Mdm2-mediated p53 degradation are presented. The consistent failure to fully protect p53 protein from E6-mediated degradation by disrupting the ubiquitin-degradation pathway provides the first evidence of an E6-dependent, ubiquitin-independent, p53 degradation pathway in vivo.

PMID:
17224909
PMCID:
PMC2742713
DOI:
10.1038/sj.onc.1210188
[Indexed for MEDLINE]
Free PMC Article

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