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A more recent version of this article appeared on April 1, 2008
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Submitted on September 21, 2007
Revised on January 16, 2008
Accepted on January 30, 2008
*Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan;
Department of Pediatric Oncology, Dana-Farber Cancer Institute and Division of Hematology/Oncology, Children’s Hospital Boston and Harvard Medical School, Boston, MA 02115;
Department of Microbiology and Immunology, Keio University School of Medicine, Tokyo 160-8582, Japan;
Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan
Monitoring Editor: Mark Solomon
Rho1p is an essential small GTPase that plays a key role in the morphogenesis of S. cerevisiae. We show here that the activation of Rho1p is regulated by a cyclin-dependent kinase (CDK). Rho1p is activated at the G1/S transition at the incipient-bud sites by the Cln2p (G1 cyclin) and Cdc28p (CDK) complex, in a process mediated by Tus1p, a guanine nucleotide exchange factor for Rho1p. Tus1p interacts physically with Cln2p/Cdc28p and is phosphorylated in a Cln2p/Cdc28p-dependent manner. CDK phosphorylation consensus sites in Tus1p are required for both Cln2p-dependent activation of Rho1p and polarized organization of the actin cytoskeleton. We propose that Cln2p/Cdc28p-dependent phosphorylation of Tus1p is required for appropriate temporal and spatial activation of Rho1p at the G1/S transition.
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