Cell cycle phosphorylation of mitotic exit network (MEN) proteins

Michele H. Jones, Jamie M. Keck, Catherine C.L. Wong, Tao Xu, John R. Yates, Mark Winey

Research output: Contribution to journalReview articlepeer-review

15 Scopus citations


Phosphorylation of proteins is an important mechanism used to regulate most cellular processes. Recently we completed an extensive phosphoproteomic analysis of the core proteins that constitute the Saccharomyces cerevisiae centrosome. Here we present a study of phosphorylation sites found on the mitotic exit network (MEN) proteins, most of which are associated with the cytoplasmic face of the centrosome. We identified 55 sites on Bfa1, Cdc5, Cdc14 and Cdc15. Eight sites lie in cyclin-dependent kinase motifs (Cdk, S/T-P), and 22 sites are completely conserved within fungi. More than half of the sites were found in centrosomes from mitotic cells, possibly in preparation for their roles in mitotic exit. Finally, we report phosphorylation site information for other important cell cycle and regulatory proteins.

Original languageEnglish (US)
Pages (from-to)3435-3440
Number of pages6
JournalCell Cycle
Issue number20
StatePublished - Oct 31 2011
Externally publishedYes


  • Cdk (cyclin-dependent kinase)/Cdc28
  • Cell cycle
  • In vivo phosphorylation
  • Mitotic exit network (MEN)
  • Plk1 (polo-like kinase)/Cdc5
  • Protein kinase
  • Yeast centrosome

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology


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