Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer.

@article{Basbous2007UbiquitinindependentPD,
  title={Ubiquitin-independent proteasomal degradation of Fra-1 is antagonized by Erk1/2 pathway-mediated phosphorylation of a unique C-terminal destabilizer.},
  author={Jihane Basbous and Dany Chalbos and R. A. Hipskind and Isabelle Jariel-Encontre and Marc Piechaczyk},
  journal={Molecular and cellular biology},
  year={2007},
  volume={27 11},
  pages={3936-50}
}
Fra-1, a transcription factor that is phylogenetically and functionally related to the proto-oncoprotein c-Fos, controls many essential cell functions. It is expressed in many cell types, albeit with differing kinetics and abundances. In cells reentering the cell cycle, Fra-1 expression is transiently stimulated albeit later than that of c-Fos and for a longer time. Moreover, Fra-1 overexpression is found in cancer cells displaying high Erk1/2 activity and has been linked to tumorigenesis. One… CONTINUE READING

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