Functional similarity between E6 proteins of cutaneous human papillomaviruses and the adenovirus E1A tumor-restraining module

J Virol. 2013 Jul;87(13):7781-6. doi: 10.1128/JVI.00037-13. Epub 2013 May 1.

Abstract

The adenovirus E1A C-terminal region restrains oncogenic transformation through interaction with three distinct cellular protein complexes that include the DYRK1A/1B/HAN11 complex. The E6 proteins of beta-human papillomaviruses (beta-HPVs) also interact with the DYRK1/HAN11 complex. A variant of HPV5 E6 frequently found in epidermodysplasia verruciformis skin lesions interacted less efficiently with DYRK1A/HAN11. The E6 variant and E7 of HPV5 efficiently coimmortalized primary epithelial cells, suggesting that naturally arising variants may contribute potential oncogenic activities of beta-HPV E6 proteins.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism
  • Adenovirus E1A Proteins / genetics
  • Adenovirus E1A Proteins / metabolism*
  • Amino Acid Sequence
  • Betapapillomavirus / metabolism*
  • Blotting, Western
  • Cell Transformation, Neoplastic / metabolism*
  • Dyrk Kinases
  • Humans
  • Immunoprecipitation
  • Molecular Sequence Data
  • Multiprotein Complexes / genetics
  • Multiprotein Complexes / metabolism*
  • Oncogene Proteins, Viral / genetics
  • Oncogene Proteins, Viral / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism
  • Sequence Homology
  • Virus Replication / genetics

Substances

  • Adaptor Proteins, Signal Transducing
  • Adenovirus E1A Proteins
  • DCAF7 protein, human
  • E6 protein, human papillomavirus type 5
  • Multiprotein Complexes
  • Oncogene Proteins, Viral
  • Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases