HPV E6, E6AP and cervical cancer

BMC Biochem. 2008 Oct 21;9 Suppl 1(Suppl 1):S4. doi: 10.1186/1471-2091-9-S1-S4.

Abstract

Every year, approximately 470,000 new cases of cervical cancer are diagnosed and approximately 230,000 women worldwide die of the disease, with the majority (approximately 80%) of these cases and deaths occurring in developing countries. Human papillomaviruses (HPVs) are the etiological agents in nearly all cases (99.7%) of cervical cancer, and the HPV E6 protein is one of two viral oncoproteins that is expressed in virtually all HPV-positive cancers. E6 hijacks a cellular ubiquitin ligase, E6AP, resulting in the ubiquitylation and degradation of the p53 tumor suppressor, as well as several other cellular proteins. While the recent introduction of prophylactic vaccines against specific HPV types offers great promise for prevention of cervical cancer, there remains a need for therapeutics. Biochemical characterization of E6 and E6AP has suggested approaches for interfering with the activities of these proteins that could be useful for this purpose. PUBLICATION HISTORY : Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com).

Publication types

  • Review

MeSH terms

  • Animals
  • Female
  • Humans
  • Ligands
  • Models, Molecular
  • Oncogene Proteins, Viral / chemistry
  • Oncogene Proteins, Viral / metabolism*
  • Papillomaviridae / metabolism*
  • Protein Conformation
  • Tumor Suppressor Protein p53 / metabolism
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / metabolism*
  • Ubiquitination
  • Uterine Cervical Neoplasms / drug therapy
  • Uterine Cervical Neoplasms / enzymology*
  • Uterine Cervical Neoplasms / virology*

Substances

  • E6 protein, Human papillomavirus type 6
  • Ligands
  • Oncogene Proteins, Viral
  • Tumor Suppressor Protein p53
  • UBE3A protein, human
  • Ubiquitin-Protein Ligases