Essential functions of Sds22p in chromosome stability and nuclear localization of PP1

Mark Peggie, Sarah MacKelvie, Andrew Bloecher, Elena Knatko, Kelly Tatchell, Michael Stark

    Research output: Contribution to journalArticle

    39 Citations (Scopus)

    Abstract

    Sds22p is a conserved, leucine-rich repeat protein that interacts with the catalytic subunit of protein phosphatase 1 (PP1C) and which has been proposed to regulate one or more functions of PP1C during mitosis. Here we show that Saccharomyces cerevisiae Sds22p is a largely nuclear protein, most of which is present as a stable 1:1 complex with yeast PP1C (Glc7p). Temperature-sensitive (Ts–) S.cerevisiae sds22 mutants show profound chromosome instability at elevated growth temperatures but do not confer a cell cycle stage-specific arrest. In the sds22-6 Ts– mutant, nuclear Glc7p is both reduced in level and aberrantly localized at 37°C and the interaction between Glc7p and Sds22p in vitro is reduced at higher temperatures, consistent with the in vivo Ts– growth defect. Like some glc7 mutations, sds22-6 can suppress the Ts– growth defect associated with ipl1-2, a loss of function mutation in a protein kinase that is known to work in opposition to PP1 on at least two nuclear substrates. This,together with reciprocal genetic interactions between GLC7 and SDS22, suggests that Sds22p functions positively with Glc7p to promote dephosphorylation of nuclear substrates required for faithful transmission of chromosomes during mitosis, and this role is at least partly mediated by effects of Sds22p on the nuclear distribution of Glc7p
    Original languageEnglish
    Pages (from-to)195-206
    Number of pages12
    JournalJournal of Cell Science
    Volume115
    Issue number1
    Publication statusPublished - 2002

    Keywords

    • Protein phosphatase 1
    • SDS22
    • GLC7

    Fingerprint Dive into the research topics of 'Essential functions of Sds22p in chromosome stability and nuclear localization of PP1'. Together they form a unique fingerprint.

  • Cite this