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.
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
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
Genes Dev.
Date: Sep. 01, 1998
PubMed ID: 9732264
View in: Pubmed Google Scholar
Download Curated Data For This Publication
8093
Switch View:
- Interactions 3
- PTM Genes 1