Logo image
Papillomavirus E6 oncoproteins
Journal article   Open access   Peer reviewed

Papillomavirus E6 oncoproteins

Scott B Vande Pol and Aloysius J Klingelhutz
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
url
https://doi.org/10.1016/j.virol.2013.04.026View
Published (Version of record) Open Access

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

Details

Logo image