@article{mbs:/content/journal/jgv/10.1099/vir.0.80035-0, author = "Grm, Helena Sterlinko and Banks, Lawrence", title = "Degradation of hDlg and MAGIs by human papillomavirus E6 is E6-AP-independent", journal= "Journal of General Virology", year = "2004", volume = "85", number = "10", pages = "2815-2819", doi = "https://doi.org/10.1099/vir.0.80035-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80035-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "An important characteristic of the E6 proteins derived from cancer-associated human papillomaviruses (HPVs) is their ability to target cellular proteins for ubiquitin-mediated degradation. Degradation of the p53 tumour suppressor protein by E6 is known to involve the cellular ubiquitin ligase, E6-AP; however, it is presently not known how E6 targets the Drosophila discs large (Dlg) tumour suppressor and the membrane-associated guanylate kinase inverted (MAGI) family of proteins for degradation. By using an in vitro E6-AP immunodepletion assay, these targets were tested for degradation in a E6-AP-dependent manner. The data showed clearly that E6 can direct the degradation of Dlg and the MAGI family of proteins in the absence of E6-AP in this in vitro system. These results provide compelling evidence for the role of E6-associated ubiquitin ligases other than E6-AP in the degradation of certain E6 targets.", }