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The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Binding of high-risk human papillomavirus E6 oncoproteins to the human homologue of the Drosophila discs large tumor suppressor protein

Kiyono, Tohru, Hiraiwa, Atsuro, Fujita, Masatoshi, Hayashi, Yasuyuki, Akiyama, Tetsu, Ishibashi, Masahide·1997·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.94.21.11612
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Abstract

In the majority of cervical cancers, DNAs of high-risk mucosotpropic human papillomaviruses (HPVs), such as type 16, are maintained so as to express two viral proteins, E6 and E7, suggesting an essential importance to carcinogenesis. The high-risk HPV E6 proteins are known to inactivate p53 tumor suppressor protein but appear to have an additional, molecularly unknown function(s). In this study, we demonstrate that these E6 proteins can bind to the second PDZ domain of the human homologue of the Drosophila discs large tumor suppressor protein (hDLG) through their C-terminal XS/TXV/L (where X represents any amino acid, S/T serine or threonine, and V/L valine or leucine) motif. This finding is similar to the interaction between the adenomatous polyposis coli gene product and hDLG. E6 mutants losing the ability to bind to hDLG are no longer able to induce E6-dependent transformation of rodent cells. These results suggest an intriguing possibility that interaction between the E6 protein and hDLG or other PDZ domain-containing proteins could be an underlying mechanism in the development of HPV-associated cancers.

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Cited by

Metadata

Authors
Kiyono, T., Hiraiwa, A., Fujita, M., Hayashi, Y., Akiyama, T., & Ishibashi, M.
Affiliations
Laboratory of Viral Oncology, Aichi Cancer Center, Research Institute, 1-1 Kanokoden, Chikusa-ku, Nagoya 464, Japan; Department of Dermatology, Nagoya University, School of Medicine, Nagoya 466, Japan; and Department of Oncogene Research, Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1997-10-14
Volume
94
Issue
21
Pages
11612-11616
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.94.21.11612
Cited by
428
References
4
Language
en

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