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Complex mechanisms for c-fos and c-jun degradation

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Abstract

c-fos and c-jun proto-oncogenes have originally been found in mutated forms in murine and avian oncogenic retroviruses. They both define multigenic families of transcription factors. Both c-jun and c-fos proteins are metabolically unstable. In vivo and in vitro work by various groups suggests that multiple proteolytic machineries, including the lysosomes, the proteasome and the ubiquitous calpains, may participate in the destruction of c-fos and c-jun. The relative contribution of each pathway is far from being known and it cannot be excluded that it varies according to the cell context and/or the physiological conditions. It has been demonstrated that, in certain occurrences, the degradation of both c-fos and c-jun by the proteasome in vivo involves the ubiquitin pathway. However, the possibility that proteasomal degradation can also occur in a manner independent of the E1 enzyme of the ubiquitin cycle remains an open issue.

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Authors and Affiliations

  1. Institute of Molecular Genetics, UMR 5535, CNRS, Route de Mende, BP5051, 34033, Montpellier, Cedex 05, France

    Isabelle Jariel-Encontre, Catherine Salvat, Ann-Muriel Steff, Magali Pariat, Claire Acquaviva, Olivia Furstoss & Marc Piechaczyk

Authors
  1. Isabelle Jariel-Encontre
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  2. Catherine Salvat
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  3. Ann-Muriel Steff
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  4. Magali Pariat
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  5. Claire Acquaviva
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  6. Olivia Furstoss
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  7. Marc Piechaczyk
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Jariel-Encontre, I., Salvat, C., Steff, AM. et al. Complex mechanisms for c-fos and c-jun degradation. Mol Biol Rep 24, 51–56 (1997). https://doi.org/10.1023/A:1006804723722

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