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p300/MDM2 complexes participate in MDM2-mediated p53 degradation.

Control of p53 turnover is critical to p53 function. E1A binding to p300/CBP translates into enhanced p53 stability, implying that these coactivator proteins normally operate in p53 turnover control. In this regard, the p300 C/H1 region serves as a specific in vivo binding site for both p53 and MDM2, a naturally occurring p53 destabilizer. Moreover, most of the endogenous MDM2 is bound to p300, and genetic analysis implies that specific interactions of p53 and MDM2 with p300 C/H1 are important steps in the MDM2-directed turnover of p53. A specific role for p300 in endogenous p53 degradation is underscored by the p53-stabilizing effect of overproducing the p300 C/H1 domain. Taken together, the data indicate that specific interactions between p300/CBP C/H1, p53, and MDM2 are intimately involved in the MDM2-mediated control of p53 abundance.

Pubmed ID: 9809062


  • Grossman SR
  • Perez M
  • Kung AL
  • Joseph M
  • Mansur C
  • Xiao ZX
  • Kumar S
  • Howley PM
  • Livingston DM


Molecular cell

Publication Data

October 1, 1998

Associated Grants


Mesh Terms

  • Cell Line
  • DNA-Binding Proteins
  • Humans
  • Molecular Sequence Data
  • Mutagenesis
  • Neoplasm Proteins
  • Nuclear Proteins
  • Oncogene Proteins, Viral
  • Protein Binding
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-mdm2
  • Sequence Homology, Amino Acid
  • Trans-Activators
  • Tumor Suppressor Protein p53
  • Ubiquitins