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Stabilization of HPV16 E6 protein by PDZ proteins, and potential implications for genome maintenance

Nicolaides, Lietta, Davy, Clare, Raj, Kenneth, Kranjec, Christian, Banks, Lawrence, Doorbar, John·2011·Virology
DOI 10.1016/j.virol.2011.03.017
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Abstract

The E6 protein from high-risk human papillomaviruses appears necessary for persistence of viral episomes in cells but the underlying mechanism is unclear. E6 has many activities, including its ability to bind and degrade PDZ domain-containing proteins, such as hScrib. However little is known about the role of these interactions for E6 function and the viral life cycle. We now show that the levels of expression of wild-type E6 are increased in the presence of hScrib whilst a mutant E6 protein lacking the PDZ-binding motif is found at lower levels as it is turned over more rapidly by the proteasome. This correlates with an inability of genomes containing this mutation to be maintained as episomes. These results show that E6 association with certain PDZ domain-containing proteins can stabilize the levels of E6 expression and provides one explanation as to how the PDZ-binding capacity of E6 might contribute to genome episomal maintenance.

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Metadata

Authors
Nicolaides, L., Davy, C., Raj, K., Kranjec, C., Banks, L., & Doorbar, J.
Venue
Virology
Publisher
Elsevier BV
Published
2011-06
Volume
414
Issue
2
Pages
137-145
ISSN
0042-6822
DOI
10.1016/j.virol.2011.03.017
Cited by
53
References
4
Language
en
Licence
Funders
  • United Kingdom Medical Research Council (U117584278, U117573807)
  • Associazione Italiana per la Ricerca sul Cancro

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