Papillomavirus E6 Oncoproteins

Virology. 2013 Oct;445(1-2):115-37. doi: 10.1016/j.virol.2013.04.026. Epub 2013 May 24.

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.

Keywords: Cervical cancer; Notch; P53; Papillomavirus; Telomerase; Transformation; Ubiquitin; Viral oncogenes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Female
  • Humans
  • Oncogene Proteins, Viral / genetics
  • Oncogene Proteins, Viral / metabolism*
  • Papillomaviridae / genetics
  • Papillomaviridae / metabolism*
  • Papillomavirus Infections / metabolism
  • Papillomavirus Infections / pathology*
  • Paxillin / metabolism
  • Protein Binding
  • Protein Folding
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitination
  • Uterine Cervical Neoplasms / pathology
  • Uterine Cervical Neoplasms / virology

Substances

  • E6 protein, Human papillomavirus type 11
  • Oncogene Proteins, Viral
  • PXN protein, human
  • Paxillin
  • UBE3A protein, human
  • Ubiquitin-Protein Ligases