Journal article
Papillomavirus E6 oncoproteins
Virology (New York, N.Y.), Vol.445(1-2), pp.115-137
10/2013
DOI: 10.1016/j.virol.2013.04.026
PMCID: PMC3783570
PMID: 23711382
Abstract
Papillomaviruses induce benign and malignant epithelial tumors, and the viral E6 oncoprotein is essential for full transformation. E6 contributes to transformation by associating with cellular proteins, docking on specific acidic LXXLL peptide motifs found on these proteins. This review examines insights from recent studies of human and animal E6 proteins that determine the three-dimensional structure of E6 when bound to acidic LXXLL peptides. The structure of E6 is related to recent advances in the purification and identification of E6 associated protein complexes. These E6 protein-complexes, together with other proteins that bind to E6, alter a broad array of biological outcomes including modulation of cell survival, cellular transcription, host cell differentiation, growth factor dependence, DNA damage responses, and cell cycle progression.
Details
- Title: Subtitle
- Papillomavirus E6 oncoproteins
- Creators
- Scott B Vande Pol - Department of Pathology, University of Virginia, Charlottesville, VA 22901, USA. Electronic address: vandepol@virginia.eduAloysius J Klingelhutz
- Resource Type
- Journal article
- Publication Details
- Virology (New York, N.Y.), Vol.445(1-2), pp.115-137
- DOI
- 10.1016/j.virol.2013.04.026
- PMID
- 23711382
- PMCID
- PMC3783570
- NLM abbreviation
- Virology
- ISSN
- 0042-6822
- eISSN
- 1096-0341
- Publisher
- United States
- Grant note
- AG027388 / NIA NIH HHS R01 CA120352 / NCI NIH HHS CA120352 / NCI NIH HHS R01 AG027388 / NIA NIH HHS P30 CA044579 / NCI NIH HHS R21 DE019953 / NIDCR NIH HHS DE019953 / NIDCR NIH HHS CA08093 / NCI NIH HHS R01 CA134737 / NCI NIH HHS
- Language
- English
- Date published
- 10/2013
- Academic Unit
- Microbiology and Immunology; Radiation Oncology
- Record Identifier
- 9984001216302771
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