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JNK targets p53 ubiquitination and degradation in nonstressed cells.

Genes & development | Sep 1, 1998

http://www.ncbi.nlm.nih.gov/pubmed/9732264

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 RIS Download

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

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Associated grants

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

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