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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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Original languageEnglish
Pages (from-to)516-519
Number of pages4
JournalScience
Volume305
Issue number5683
DOIs
StatePublished - 2004

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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