Extra Views

Cell cycle phosphorylation of mitotic exit network (MEN) proteins

Volume 10, Issue 20   October 15, 2011
Pages 3435 - 3440
http://dx.doi.org/10.4161/cc.10.20.17790
Keywords: In vivo phosphorylation, Cdk (cyclin-dependent kinase)/Cdc28, Mitotic Exit Network (MEN), Plk1 (polo-like kinase)/Cdc5, cell cycle, protein kinase, yeast centrosome
Authors: Michele H. Jones, Jamie M. Keck, Catherine C. L. Wong, Tao Xu, John R. Yates and Mark Winey

View affiliations

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.

Received: August 10, 2011; Accepted: August 17, 2011

Preview:



Advertisements