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

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

    Research output: Contribution to journalArticle

    132 Citations (Scopus)

    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.

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

    Cite this

    Azzam, R., Chen, S. L., Shou, W., Mah, A. S., Alexandru, G., Nasmyth, K., Annan, R. S., Carr, S. A., & Deshaies, R. J. (2004). Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus. Science, 305(5683), 516-519. https://doi.org/10.1126/science.1099402