HAUSP/USP7 as an Epstein-Barr virus target

Biochem Soc Trans. 2004 Nov;32(Pt 5):731-2. doi: 10.1042/BST0320731.

Abstract

USP7 (also called HAUSP) is a de-ubiquitinating enzyme recently identified as a key regulator of the p53-mdm2 pathway, which stabilizes both p53 and mdm2. We have discovered that the Epstein-Barr nuclear antigen 1 protein of Epstein-Barr virus binds with high affinity to USP7 and disrupts the USP7-p53 interaction. The results have important implications for the role of Epstein-Barr nuclear antigen 1 in the cellular immortalization that is typical of an Epstein-Barr virus latent infection.

Publication types

  • Review

MeSH terms

  • Animals
  • Catalytic Domain
  • Cell Line, Tumor
  • Endopeptidases / metabolism
  • Endopeptidases / physiology*
  • Herpesvirus 4, Human / metabolism*
  • Humans
  • Mice
  • Models, Biological
  • Nuclear Proteins / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-mdm2
  • Tumor Suppressor Protein p53 / metabolism
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Peptidase 7

Substances

  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Tumor Suppressor Protein p53
  • MDM2 protein, human
  • Mdm2 protein, mouse
  • Proto-Oncogene Proteins c-mdm2
  • Endopeptidases
  • USP7 protein, human
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Peptidase 7