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Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus

Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus

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Authors

  • Ramzi Azzam
  • Susan L. Chen
  • Wenying Shou
  • Angie S. Mah
  • Gabriela Alexandru
  • Kim Nasmyth
  • Roland S. Annan
  • Steven A. Carr
  • Raymond J. Deshaies

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Info

Original languageEnglish
Pages516-519
Number of pages4
JournalScience
Journal publication date2004
Journal number5683
Volume305
DOIs
StatePublished

Abstract

Budding yeast protein phosphatase Cdc14 is sequestered in the nucleolus in an inactive state during interphase by the anchor protein Net1. Upon entry into anaphase, the Cdc14 early anaphase release ( FEAR) network initiates dispersal of active Cdc14 throughout the cell. We report that the FEAR network promotes phosphorylation of Net1 by cyclin-dependent kinase (Cdk) complexed with cyclin B1 or cyclin B2. These phosphorylations appear to be required for FEAR and sustain the proper timing of late mitotic events. Thus, a regulatory circuit exists to ensure that the arbiter of the mitotic state, Cdk, sets in motion events that culminate in exit from mitosis.

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