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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53.

The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the presence of E1, UbcH5 as E2 and MDM2 oncoprotein. A ubiquitin molecule bound MDM2 through sulfhydroxy bond which is characteristic of ubiquitin ligase (E3)-ubiquitin binding. The cysteine residue in the carboxyl terminus of MDM2 was essential for the activity. These data suggest that the MDM2 protein, which is induced by p53, functions as a ubiquitin ligase, E3, in human papillomavirus-uninfected cells which do not have E6 protein.

Pubmed ID: 9450543

Authors

  • Honda R
  • Tanaka H
  • Yasuda H

Journal

FEBS letters

Publication Data

December 22, 1997

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Cell Extracts
  • HeLa Cells
  • Humans
  • Ligases
  • Molecular Sequence Data
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-mdm2
  • Sequence Analysis
  • Tumor Suppressor Protein p53
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitins