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The Human Papillomavirus Type 16 E6 Oncoprotein Can Down-Regulate p53 Activity by Targeting the Transcriptional Coactivator CBP/p300

Zimmermann, Holger, Degenkolbe, Roland, Bernard, Hans-Ulrich, O’Connor, Mark J.·1999·Journal of Virology
DOI 10.1128/jvi.73.8.6209-6219.1999
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Abstract

The transforming proteins of the small DNA tumor viruses, simian virus 40 (SV40), adenovirus, and human papillomavirus (HPV) target a number of identical cellular regulators whose functional abrogation is required for transformation. However, while both adenovirus E1A and SV40 large T transforming properties also depend on the targeting of the transcriptional coactivator CBP/p300, no such interaction has been described for the HPV oncoprotein E6 or E7. Here, we demonstrate that the HPV-16 E6 protein, previously shown to facilitate the degradation of p53 in a complex with E6-associated protein (E6AP), also targets CBP/p300 in an interaction involving the C-terminal zinc finger of E6 and CBP residues 1808 to 1826. Furthermore, this interaction is limited to E6 proteins of high-risk HPVs associated with cervical cancer that have the capacity to repress p53-dependent transcription. An HPV-16 E6 mutant (L50G) that binds CBP/p300, but not E6AP, is still capable of down-regulating p53 transcriptional activity. Thus, HPV E6 proteins possess two distinct mechanisms by which to abrogate p53 function: the repression of p53 transcriptional activity by targeting the p53 coactivator CBP/p300, and the removal of cellular p53 protein through the proteosome degradation pathway.

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Cited by

Metadata

Authors
Zimmermann, H., Degenkolbe, R., Bernard, H.-U., & O’Connor, M. J.
Affiliations
<!--label omitted: 1-->Institute of Molecular and Cell Biology, Singapore 117 609, Singapore
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
1999-08
Volume
73
Issue
8
Pages
6209-6219
ISSN
  • 0022-538X
  • 1098-5514
DOI
10.1128/jvi.73.8.6209-6219.1999
Cited by
282
References
5
Language
en
Licence
journals.asm.org/non-commercial-tdm-license (tdm)

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