The life cycle of C-myc: from synthesis to degradation

Cell Cycle. 2004 Sep;3(9):1133-7. Epub 2004 Sep 5.


The c-Myc transcription factor is a potent regulator of cellular proliferation and cell fate decision. Precise regulation of c-Myc protein levels is essential to maintain normal cell function. In order to maintain proper levels of c-Myc, its protein stability is tightly controlled. c-Myc is degraded through the ubiquitin-proteasome pathway. This perspective discusses a sophisticated and complex signaling pathway that controls the life cycle of c-Myc from protein synthesis to ubiquitin-mediated degradation. The pathway involves Ras-activated kinases, the Pin1 prolyl isomerase, the PP2A phosphatase and a series of c-Myc phosphorylation and dephosphorylation events that control its stability.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Humans
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptidylprolyl Isomerase / metabolism
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Transport / physiology
  • Proto-Oncogene Proteins c-myc / biosynthesis*
  • Proto-Oncogene Proteins c-myc / genetics*
  • Signal Transduction / physiology*
  • Ubiquitin / metabolism*
  • ras Proteins / metabolism


  • MYC protein, human
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Proto-Oncogene Proteins c-myc
  • Ubiquitin
  • Phosphoprotein Phosphatases
  • Proteasome Endopeptidase Complex
  • ras Proteins
  • PIN1 protein, human
  • Peptidylprolyl Isomerase