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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Humans
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NIMA-Interacting Peptidylprolyl Isomerase
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Peptidylprolyl Isomerase / metabolism
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Phosphoprotein Phosphatases / metabolism
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Phosphorylation
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Proteasome Endopeptidase Complex / metabolism*
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Protein Transport / physiology
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Proto-Oncogene Proteins c-myc / biosynthesis*
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Proto-Oncogene Proteins c-myc / genetics*
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Signal Transduction / physiology*
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Ubiquitin / metabolism*
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ras Proteins / metabolism
Substances
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MYC protein, human
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NIMA-Interacting Peptidylprolyl Isomerase
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Proto-Oncogene Proteins c-myc
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Ubiquitin
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Phosphoprotein Phosphatases
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Proteasome Endopeptidase Complex
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ras Proteins
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PIN1 protein, human
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Peptidylprolyl Isomerase