Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 282, Issue 8, Pages 5432-5442Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M611437200
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Funding
- NCI NIH HHS [K01 CA086957, K01 CA086957-06, R01 CA100855, R01 CA100855-03] Funding Source: Medline
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The c-Myc transcription factor is a key regulator of cell proliferation and cell fate decisions. c-Myc overexpression is observed in a variety of human tumors, revealing the importance of maintaining normal levels of c-Myc protein. c-Myc protein stability in mammalian cells is controlled by interdependent and sequential phosphorylation and dephosphorylation events on two highly conserved residues, serine 62 and threonine 58. Here we show that these sequential phosphorylation and dephosphorylation events and their effect on c-Myc stability also occurs in the model system Saccharomyces cerevisiae. These results suggest the presence of a conserved pathway in yeast that controls protein turnover in response to a specific phospho-degron sequence. These findings have implications regarding conserved pathways for regulated protein degradation, and they validate the use of genetically tractable yeast for the study of the turnover of proteins such as c-Myc that contain this motif.
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