Orchestrating anaphase and mitotic exit: separase cleavage and localization of Slk19

Nat Cell Biol. 2001 Sep;3(9):771-7. doi: 10.1038/ncb0901-771.


Anaphase in budding yeast is triggered by cleavage of the central subunit, Scc1, of the chromosomal cohesin complex by the protease separase. Here we show that separase also cleaves the kinetochore-associated protein Slk19 at anaphase onset. Separase activity is also required for the proper localization of a stable Slk19 cleavage product to the spindle midzone in anaphase. The cleavage and localization of Slk19 are necessary to stabilize the anaphase spindle, and we show that a stable spindle is a prerequisite for timely exit from mitosis. This demonstrates the cleavage of targets other than cohesin by separase in the orchestration of high-fidelity anaphase.

MeSH terms

  • Amino Acid Sequence
  • Anaphase / physiology
  • Binding Sites
  • Cell Cycle / physiology*
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Division / physiology*
  • Chromosomal Proteins, Non-Histone
  • Endopeptidases*
  • Kinetics
  • Kinetochores / physiology
  • Microtubule-Associated Proteins / genetics*
  • Microtubule-Associated Proteins / metabolism*
  • Mitosis / physiology
  • Molecular Sequence Data
  • Nuclear Proteins
  • Phosphoproteins
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins*
  • Separase
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • MCD1 protein, S cerevisiae
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • Phosphoproteins
  • Saccharomyces cerevisiae Proteins
  • Slk19 protein, S cerevisiae
  • Endopeptidases
  • ESP1 protein, S cerevisiae
  • Separase