Mitotic exit network controls the localization of Cdc14 to the spindle pole body in Saccharomyces cerevisiae

Curr Biol. 2002 Jun 4;12(11):944-50. doi: 10.1016/s0960-9822(02)00870-9.

Abstract

Budding yeast Cdc14 phosphatase plays essential roles in mitotic exit. Cdc14 is sequestered in the nucleolus by its inhibitor Net1/Cfi1 and is only released from the nucleolus during anaphase to inactivate mitotic CDK. It is believed that the mitotic exit network (MEN) is required for the release of Cdc14 from the nucleolus because liberation of Cdc14 by net1/cfi1 mutations bypasses the essential role of the MEN. But how the MEN residing at the spindle pole body (SPB) controls the association of Cdc14 with Net1/Cfi1 in the nucleolus is not yet understood. We found that Cdc14-5GFP was released from the nucleolus in the MEN mutants (tem1, cdc15, dbf2, and nud1), but not in the cdc5 cells during early anaphase. The Cdc14 liberation from the nucleolus was inhibited by the Mad2 checkpoint and by the Bub2 checkpoint in a different manner when microtubule organization was disrupted. We observed Cdc14-5GFP at the SPB in addition to the nucleolus. The SPB localization of Cdc14 was significantly affected by the MEN mutations and the bub2 mutation. We conclude that Cdc14 is released from the nucleolus at the onset of anaphase in a CDC5-dependent manner and that MEN factors possibly regulate Cdc14 release from the SPB.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / metabolism*
  • Fungal Proteins / metabolism*
  • Green Fluorescent Proteins
  • Luminescent Proteins / metabolism
  • Mitosis*
  • Protein Tyrosine Phosphatases*
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae Proteins*
  • Spindle Apparatus / metabolism*

Substances

  • CDC14 protein, S cerevisiae
  • Cell Cycle Proteins
  • Fungal Proteins
  • Luminescent Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Green Fluorescent Proteins
  • Protein Tyrosine Phosphatases