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A more recent version of this article appeared on April 1, 2008
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Submitted on July 28, 2007
Revised on January 17, 2008
Accepted on January 29, 2008
Instituto de Microbiología Bioquímica, Consejo Superior de Investigaciones Científicas (CSIC) / Departamento de Microbiología y Genética. Universidad de Salamanca. Edificio Departamental 37007 Salamanca, Spain
Monitoring Editor: Daniel Lew
Schizosaccharomyces pombe Rho GTPases regulate actin cytoskeleton organization and cell integrity. We studied the fission yeast gene SPBC4F6.12 based on its ability to suppress the thermosensitivity of cdc42-1625 mutant strain. This gene, named pxl1+, encodes a protein with three LIM domains that is similar to paxillin. Pxl1 does not interact with Cdc42 but it interacts with Rho1, and negatively regulates this GTPase. Fission yeast Pxl1 forms a contractile ring in the cell division region and deletion of pxl1+ causes a delay in cell-cell separation suggesting that it has a function in cytokinesis. Pxl1 N-terminal region is required and sufficient for its localization to the medial ring whereas the LIM domains are necessary for its function. Pxl1 localization requires actin polymerization and the actomyosin ring but is independent of the septation initiation network (SIN) function. Moreover, Pxl1 colocalizes and interacts with Myo2, and Cdc15, suggesting that it is part of the actomyosin ring. Here we show that in cells lacking Pxl1, the myosin ring is not correctly assembled and that actomyosin ring contraction is delayed. All together these data suggest that Pxl1 modulates Rho1 GTPase signaling, and plays a role in the formation and contraction of the actomyosin ring during cytokinesis.
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