Abstract
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.
Original language | English (US) |
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Pages (from-to) | 1131-1135 |
Number of pages | 5 |
Journal | Cell Cycle |
Volume | 3 |
Issue number | 9 |
DOIs | |
State | Published - Sep 2004 |
Keywords
- ERK
- GSK-3β
- PP2A
- Pin1
- Ras
- Serine 62
- Stability
- Threonine 58
- c-Myc
ASJC Scopus subject areas
- Molecular Biology
- Developmental Biology
- Cell Biology