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Vol. 13, Issue 10, 3532-3545, October 2002
Programme in Cell Biology, Hospital for Sick Children and
Department of Biochemistry, University of Toronto, Toronto, Ontario M5G
1X8, Canada
Cytokinesis in animal cells involves the contraction of an
actomyosin ring formed at the cleavage furrow. Nuclear division, or
karyokinesis, must be precisely timed to occur before cytokinesis in
order to prevent genetic anomalies that would result in either cell
death or uncontrolled cell division. The septin family of GTPase
proteins has been shown to be important for cytokinesis although little
is known about their role during this process. Here we investigate the
distribution and function of the mammalian septin MSF. We show that
during interphase, MSF colocalizes with actin, microtubules, and
another mammalian septin, Nedd5, and coprecipitates with six septin
proteins. In addition, transfections of various MSF isoforms reveal
that MSF-A specifically localizes with microtubules and that this
localization is disrupted by nocodazole treatment. Furthermore, MSF
isoforms localize primarily with tubulin at the central spindle during
mitosis, whereas Nedd5 is mainly associated with actin. Microinjection
of affinity-purified anti-MSF antibodies into synchronized cells, or
depletion of MSF by small interfering RNAs, results in the accumulation
of binucleated cells and in cells that have arrested during
cytokinesis. These results reveal that MSF is required for the
completion of cytokinesis and suggest a role that is distinct from that
of Nedd5.
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