Year: 2004
Type: article
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.
Source: Cell Cycle
DOI: 10.4161/cc.3.9.1145
Author: Rosalie C. Sears
Institution: Oregon Health & Science University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Funder: National Cancer Institute
OpenAlex ID: W2046405795
