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.
MeSH terms
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Animals
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Catalytic Domain
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Cell Line, Tumor
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Endopeptidases / metabolism
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Endopeptidases / physiology*
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Herpesvirus 4, Human / metabolism*
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Humans
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Mice
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Models, Biological
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Nuclear Proteins / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-mdm2
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Tumor Suppressor Protein p53 / metabolism
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Ubiquitin Thiolesterase
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Ubiquitin-Specific Peptidase 7
Substances
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Nuclear Proteins
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Proto-Oncogene Proteins
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Tumor Suppressor Protein p53
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MDM2 protein, human
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Mdm2 protein, mouse
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Proto-Oncogene Proteins c-mdm2
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Endopeptidases
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USP7 protein, human
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Ubiquitin Thiolesterase
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Ubiquitin-Specific Peptidase 7