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A more recent version of this article appeared on October 1, 2002
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Submitted on January 24, 2002
Revised on June 14, 2002
Accepted on August 5, 2002
1 Programme in Cell Biology, Hospital for Sick Children and Department of Biochemistry, University of Toronto, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada
* Corresponding author. E-mail address: wtrimble{at}sickkids.on.ca.
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 prior to 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 co-localizes with actin, microtubules, and another mammalian septin, Nedd5, and co-precipitates 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 while 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 bi-nucleated 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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