Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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