Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases

Science. 1997 Jan 17;275(5298):400-2. doi: 10.1126/science.275.5298.400.


The proto-oncogene-encoded transcription factor c-Jun activates genes in response to a number of inducers that act through mitogen-activated protein kinase (MAPK) signal transduction pathways. The activation of c-Jun after phosphorylation by MAPK is accompanied by a reduction in c-Jun ubiquitination and consequent stabilization of the protein. These results illustrate the relevance of regulated protein degradation in the signal-dependent control of gene expression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Cell Cycle Proteins / metabolism
  • GTP-Binding Proteins / metabolism
  • Gene Expression Regulation
  • JNK Mitogen-Activated Protein Kinases
  • Mice
  • Mitogen-Activated Protein Kinases*
  • Phosphorylation
  • Proto-Oncogene Proteins c-jun / metabolism*
  • Signal Transduction
  • Transfection
  • Ubiquitins / metabolism*
  • cdc42 GTP-Binding Protein, Saccharomyces cerevisiae


  • Cell Cycle Proteins
  • Proto-Oncogene Proteins c-jun
  • Ubiquitins
  • Calcium-Calmodulin-Dependent Protein Kinases
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases
  • GTP-Binding Proteins
  • cdc42 GTP-Binding Protein, Saccharomyces cerevisiae