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Vol. 12, Issue 12, 3892-3903, December 2001
,*
and
*Departments of Biology and In budding yeast, actin disruption prevents nuclear division. This
has been explained as activation of a morphogenesis checkpoint monitoring the integrity of the actin cytoskeleton. The checkpoint operates through inhibitory tyrosine phosphorylation of Cdc28, the
budding yeast Cdc2 homolog. Wild-type Schizosaccharomyces pombe cells also arrest before mitosis after actin
depolymerization. Oversized cells, however, enter mitosis uninhibited.
We carried out a careful analysis of the kinetics of mitotic initiation
after actin disruption in undersized and oversized cells. We show that an inability to reach the mitotic size threshold explains the arrest in
smaller cells. Among the regulators that control the level of the
inhibitory Cdc2-Tyr15 phosphorylation, the Cdc25 protein tyrosine
phosphatase is required to link cell size monitoring to mitotic
control. This represents a novel function of the Cdc25 phosphatase.
Furthermore, we demonstrate that this cell size-monitoring system
fulfills the formal criteria of a cell cycle checkpoint.
Biochemistry, Queen's
University, Kingston, Ontario K7L 3N6, Canada
Corresponding author. E-mail address:
youngpg{at}biology.queensu.ca.
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