Regulation of p53 by Mdm2: fate is in the numbers

Mol Cell. 2004 Jan 16;13(1):4-5. doi: 10.1016/s1097-2765(03)00529-x.

Abstract

The p53 tumor suppressor protein is normally restrained by the Mdm2 oncoprotein, which promotes p53 ubiquitination. In a recent issue of Science, report that p53 may face two alternative fates, depending on Mdm2 levels: high Mdm2 drives p53 polyubiquitination and degradation within the cell nucleus, whereas low Mdm2 promotes p53 monoubiquitination and nuclear exclusion.

MeSH terms

  • Active Transport, Cell Nucleus
  • Apoptosis
  • Cell Nucleus / metabolism*
  • Cysteine Endopeptidases / metabolism
  • Cytoplasm / metabolism
  • Gene Expression Regulation*
  • Humans
  • Ligases
  • Models, Biological
  • Multienzyme Complexes / metabolism
  • Nuclear Proteins*
  • Proteasome Endopeptidase Complex
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-mdm2
  • Recombinant Fusion Proteins / metabolism
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism*
  • Ubiquitin / genetics
  • Ubiquitin / metabolism

Substances

  • Multienzyme Complexes
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Recombinant Fusion Proteins
  • Tumor Suppressor Protein p53
  • Ubiquitin
  • MDM2 protein, human
  • Proto-Oncogene Proteins c-mdm2
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Ligases