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Cell cycle phosphorylation of mitotic exit network (MEN) proteins

Academic Article
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Overview

authors

  • Jones, M. H.
  • Keck, Jamie
  • Wong, C. C. L.
  • Xu, T.
  • Yates III, John
  • Winey, M.

publication date

  • October 2011

journal

  • Cell Cycle  Journal

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.

subject areas

  • Binding Sites
  • Cell Cycle Proteins
  • Centrosome
  • Mitosis
  • Models, Biological
  • Phosphorylation
  • Proteomics
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Signal Transduction
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Research

keywords

  • Cdk (cyclin-dependent kinase)/Cdc28
  • Plk1 (polo-like kinase)/Cdc5
  • cell cycle
  • in vivo phosphorylation
  • mitotic exit network (MEN)
  • protein kinase
  • yeast centrosome
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Identity

PubMed Central ID

  • PMC3266174

International Standard Serial Number (ISSN)

  • 1538-4101

Digital Object Identifier (DOI)

  • 10.4161/cc.10.20.17790

PubMed ID

  • 22031224
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Additional Document Info

start page

  • 3435

end page

  • 3440

volume

  • 10

issue

  • 20

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