Cited by 117

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The hScrib/Dlg apico-basal control complex is differentially targeted by HPV-16 and HPV-18 E6 proteins

Thomas, Miranda, Massimi, Paola, Navarro, Christel, Borg, Jean-Paul, Banks, Lawrence·2005·Oncogene

Abstract

The E6 proteins of the high-risk Human papillomaviruses (HPV) types have a well-documented ability to target certain cellular proteins for ubiquitin-mediated degradation via the proteasome. Previous studies have shown that E6 proteins interact differently with different target proteins, and that the viral proteins, depending upon the target, may recruit diverse cellular ubiquitin-protein ligases. In this study, we have examined the abilities of E6 proteins from HPV-16 and HPV-18 to interact with and induce the degradation of two PDZ domain-containing targets, Dlg and hScrib. We have also mapped the binding site of E6 on hScrib and shown that the interaction of E6 with hScrib is distinct from its interactions with other PDZ domain-containing targets. This is reflected in the efficiency with which the two viral E6 proteins can inhibit hScrib's suppression of cell transformation.Dlg and hScrib have complementary activities in the control of epithelial cell polarity and the fact that both are targeted by high-risk HPV E6 proteins underlines their importance. Our finding that they are each targeted differently by HPV-16 and HPV-18 E 6 s suggests that the two viruses are subjected to somewhat different constraints and provides a possible explanation for the apparent redundancy in targeting both parts of this important control mechanism.

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Crossref · 10.1038/sj.onc.1208757

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4 of 4 references verified0 citation errors · 0 not checkable

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Cited by

Metadata

Authors
Thomas, M., Massimi, P., Navarro, C., Borg, J.-P., & Banks, L.
Venue
Oncogene
Published
2005-08-15
Volume
24
Issue
41
Pages
6222-6230
ISSN
  • 0950-9232
  • 1476-5594
Cited by
117
References
4
Language
en

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