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Cell cycle phosphorylation of mitotic exit network (MEN) proteins.
- Source :
-
Cell cycle (Georgetown, Tex.) [Cell Cycle] 2011 Oct 15; Vol. 10 (20), pp. 3435-40. Date of Electronic Publication: 2011 Oct 15. - Publication Year :
- 2011
-
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.
- Subjects :
- Binding Sites genetics
Centrosome metabolism
Models, Biological
Phosphorylation
Proteomics methods
Saccharomyces cerevisiae genetics
Cell Cycle Proteins metabolism
Centrosome physiology
Mitosis physiology
Saccharomyces cerevisiae physiology
Saccharomyces cerevisiae Proteins metabolism
Signal Transduction physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1551-4005
- Volume :
- 10
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- Cell cycle (Georgetown, Tex.)
- Publication Type :
- Academic Journal
- Accession number :
- 22031224
- Full Text :
- https://doi.org/10.4161/cc.10.20.17790