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A more recent version of this article appeared on November 1, 2003
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Submitted on April 17, 2003
Revised on July 10, 2003
Accepted on July 14, 2003
1 Institute of Molecular and Cell Biology, 30, Medical Drive, Singapore117609
* Corresponding author. E-mail address: mcbucs{at}imcb.nus.edu.sg.
* Corresponding author. E-mail address: mcbucs{at}imcb.nus.edu.sg.
* Corresponding author. E-mail address: mcbucs{at}imcb.nus.edu.sg.
Chromosome segregation, mitotic exit and cytokinesis are executed in this order during mitosis. Although a scheme coordinating sister chromatid separation and initiation of mitotic exit has been proposed, the mechanism that temporally links the onset of cytokinesis to mitotic exit is not known. Exit from mitosis is regulated by the Mitotic Exit Network (MEN) which includes a GTPase (Tem1) and various Kinases (Cdc15, Cdc5, Dbf2 and Dbf20). Here we show that Dbf2 and Dbf20 functions are necessary for the execution of cytokinesis. Relocalization of these proteins from spindle pole bodies (SPBs) to mother-daughter neck appears to be necessary for this role since cdc15-2 mutant cells, though capable of exiting mitosis at semipermissive temperature, are unable to localize Dbf2 (and Dbf20) to the ‘neck' and fail to undergo cytokinesis. These cells can assemble and constrict the actomyosin ring normally but are incapable of forming a septum, suggesting that MEN components are critical for the initiation of septum formation. Interestingly, the SPB-to-‘neck' translocation of Dbf2 and Dbf20 is triggered by the inactivation of mitotic kinase. The requirement of kinase inactivation for translocation of MEN components to the division site thus provides a mechanism that renders mitotic exit a prerequisite for cytokinesis.
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