Abstract
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 language | English (US) |
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Pages (from-to) | 3435-3440 |
Number of pages | 6 |
Journal | Cell Cycle |
Volume | 10 |
Issue number | 20 |
DOIs | |
State | Published - Oct 31 2011 |
Externally published | Yes |
Keywords
- 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