A conserved pathway that controls c-Myc protein stability through opposing phosphorylation events occurs in yeast

Julienne R. Escamilla-Powers, Rosalie C. Sears

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5432-5442
Number of pages11
JournalJournal of Biological Chemistry
Volume282
Issue number8
DOIs
StatePublished - Feb 23 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'A conserved pathway that controls c-Myc protein stability through opposing phosphorylation events occurs in yeast'. Together they form a unique fingerprint.

  • Cite this