Are there multiple proteolytic pathways contributing to c-Fos, c-Jun and p53 protein degradation in vivo?

Mol Biol Rep. 1999 Apr;26(1-2):45-51. doi: 10.1023/a:1006960021281.


The c-Fos and c-Jun oncoproteins and the p53 tumor suppressor protein are short-lived transcription factors. Several catabolic pathways contribute to their degradation in vivo. c-Fos and c-Jun are thus mostly degraded by the proteasome, but there is indirect evidence that, under certain experimental/physiological conditions, calpains participate in their destruction, at least to a limited extent. Lysosomes have also been reported to participate in the destruction of c-Fos. Along the same lines, p53 is mostly degraded following the ubiquitin/proteasome pathway and calpains also seem to participate in its degradation. Moreover, c-Fos, c-Jun and p53 turnovers are regulated upon activation of intracellular signalling cascades. All taken together, these observations underline the complexity of the mechanisms responsible for the selective destruction of proteins within cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Cycle
  • Cricetinae
  • Cysteine Endopeptidases / metabolism
  • Humans
  • Mice
  • Multienzyme Complexes / metabolism
  • Proteasome Endopeptidase Complex
  • Proto-Oncogene Proteins c-fos / metabolism*
  • Proto-Oncogene Proteins c-jun / metabolism*
  • Signal Transduction
  • Tumor Suppressor Protein p53 / metabolism*


  • Multienzyme Complexes
  • Proto-Oncogene Proteins c-fos
  • Proto-Oncogene Proteins c-jun
  • Tumor Suppressor Protein p53
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex