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A more recent version of this article appeared on March 1, 2002
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Submitted on August 1, 2001
Revised on December 2, 2001
Accepted on December 18, 2001
1 Cell Division Laboratory, The Institute of Molecular Agrobiology, The National University of Singapore, 1 Research Link, Singapore 117604
2 The Institute of Molecular Agrobiology, The National University of Singapore, 1 Research Link, Singapore 117604
* Corresponding author. E-mail address: jliu{at}ima.org.sg.
Schizosaccharomyces pombe cells divide by medial fission through the use of an actomyosin-based contractile ring. Constriction of the actomyosin ring is accompanied by the centripetal addition of new membranes and cell wall material. In this paper, we characterize the mechanism responsible for the localization of Cps1p, a septum-synthesizing 1,3-ß-glucan synthase, to the division site during cytokinesis. We show that Cps1p is an integral membrane protein that localizes to the cell division site late in anaphase. Neither F-actin nor microtubules are essential for the initial assembly of Cps1p to the medial division site. F-actin, but not microtubules, is however important for the eventual incorporation of Cps1p into the actomyosin ring. Assembly of Cps1p into the cell division ring is also dependent on the Septation-Inducing Network (SIN) proteins that regulate division septum formation following assembly of the actomyosin ring. Fluorescence-recovery after-photobleaching experiments reveal that Cps1p does not diffuse appreciably within the plasma membrane and is retained at the division site by a mechanism that does not depend on an intact F-actin cytoskeleton. We conclude that the actomyosin ring serves as a spatial cue for Cps1p localization, while the maintenance of Cps1p at the division site occurs by a novel F-actin and microtubule independent mechanism. Furthermore, we propose that the SIN proteins ensure localization of Cps1p at the appropriate point in the cell cycle.
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