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Vol. 12, Issue 10, 2961-2974, October 2001
Center for Cancer Research, Howard Hughes Medical Institute,
Massachusetts Institute of Technology, E17-233, 40 Ames Street,
Cambridge MA 02139
In budding yeast, the release of the protein phosphatase Cdc14 from
its inhibitor Cfi1/Net1 in the nucleolus during anaphase triggers the
inactivation of Clb CDKs that leads to exit from mitosis. The mitotic
exit pathway controls the association between Cdc14 and Cfi1/Net1. It
is comprised of the RAS-like GTP binding protein Tem1, the exchange
factor Lte1, the GTPase activating protein complex Bub2-Bfa1/Byr4, and
several protein kinases including Cdc15 and Dbf2. Here we investigate
the regulation of the protein kinases Dbf2 and Cdc15. We find that
Cdc15 is recruited to both spindle pole bodies (SPBs) during anaphase.
This recruitment depends on TEM1 but not
DBF2 or CDC14 and is inhibited by
BUB2. Dbf2 also localizes to SPBs during anaphase, which
coincides with activation of Dbf2 kinase activity. Both events depend
on the mitotic exit pathway components TEM1 and
CDC15. In cells lacking BUB2, Dbf2 localized to SPBs in cell cycle stages other than anaphase and telophase and Dbf2 kinase was prematurely active during metaphase. Our
results suggest an order of function of mitotic exit pathway components
with respect to SPB localization of Cdc15 and Dbf2 and activation of
Dbf2 kinase. BUB2 negatively regulates all 3 events.
Loading of Cdc15 on SPBs depends on TEM1, whereas
loading of Dbf2 on SPBs and activation of Dbf2 kinase depend on
TEM1 and CDC15.
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