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JNK targets p53 ubiquitination and degradation in nonstressed cells.

In this study we elucidated the role of nonactive JNK in regulating p53 stability. The amount of p53-JNK complex was inversely correlated with p53 level. A peptide corresponding to the JNK binding site on p53 efficiently blocked ubiquitination of p53. Similarly, p53 lacking the JNK binding site exhibits a longer half-life than p53(wt). Outcompeting JNK association with p53 increased the level of p53, whereas overexpression of a phosphorylation mutant form of JNK inhibited p53 accumulation. JNK-p53 and Mdm2-p53 complexes were preferentially found in G0/G1 and S/G2M phases of the cell cycle, respectively. Altogether, these data indicate that JNK is an Mdm2-independent regulator of p53 stability in nonstressed cells.

Pubmed ID: 9732264


  • Fuchs SY
  • Adler V
  • Buschmann T
  • Yin Z
  • Wu X
  • Jones SN
  • Ronai Z


Genes & development

Publication Data

September 1, 1998

Associated Grants

  • Agency: NCI NIH HHS, Id: CA59908
  • Agency: NCI NIH HHS, Id: CA78419

Mesh Terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Line
  • JNK Mitogen-Activated Protein Kinases
  • Mice
  • Mitogen-Activated Protein Kinases
  • Molecular Sequence Data
  • Nuclear Proteins
  • Peptide Fragments
  • Phosphorylation
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-mdm2
  • Recombinant Proteins
  • Reticulocytes
  • Sequence Deletion
  • Spodoptera
  • Transfection
  • Tumor Suppressor Protein p53
  • Ubiquitins