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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Association of E6AP (UBE3A) with human papillomavirus type 11 E6 protein.

The cellular E3 ubiquitin ligase E6AP (UBE3A) interacts with the cancer- associated HPV E6 oncoproteins, where together with the viral E6 oncoprotein it binds and targets the degradation of the p53 tumor suppressor. We find that the HPV-11E6 protein also associates with E6AP in vivo, and thereby can target the degradation of an E6-associated protein. Mutation of an E6- binding LXXLL peptide motif on E6AP eliminated the association, revealing a common mode of interaction between high- and low-risk E6 proteins and E6AP. E6AP was required for the in vivo degradation of DLG1 by both HVP-18 E6 and a chimeric HPV-11E6. The common functional interaction of both cancer-associated and non-cancer-associated E6 proteins with E6AP establishes a common mechanism for E6 proteins trophic to mucosal squamous epithelium.[1]


  1. Association of E6AP (UBE3A) with human papillomavirus type 11 E6 protein. Brimer, N., Lyons, C., Vande Pol, S.B. Virology (2007) [Pubmed]
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