Abstract:
:Human papillomavirus (HPV) E6 oncoproteins target numerous cellular proteins for ubiquitin-mediated degradation. In the case of p53 this is mediated by the E6AP ubiquitin ligase. However, there are conflicting reports concerning how central E6AP is to the global function of the HPV-16 and HPV-18 E6 oncoproteins. To investigate this further we have analysed the effects of E6AP removal upon the stability of endogenously expressed E6 protein. We show that when E6AP is silenced in HPV-positive cells, E6 protein levels are dramatically decreased in a proteasome-dependent manner. Further, we show that when E6AP is depleted in HeLa cells, E6 has a greatly decreased half-life. In addition, overexpression of E6AP stabilises ectopically expressed HPV-16 and HPV-18 E6 in a manner that is independent of its ubiquitin ligase activity. These results demonstrate that the stability of HPV E6 is critically dependent upon the presence of E6AP.
journal_name
Virologyjournal_title
Virologyauthors
Tomaić V,Pim D,Banks Ldoi
10.1016/j.virol.2009.07.029subject
Has Abstractpub_date
2009-10-10 00:00:00pages
7-10issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(09)00448-6journal_volume
393pub_type
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