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MBC in Press, published online ahead of print February 6, 2008
Mol. Biol. Cell 10.1091/mbc.E07-09-0950

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Submitted on September 21, 2007
Revised on January 16, 2008
Accepted on January 30, 2008

G1/S Cyclin-Dependent Kinase Regulates Small GTPase Rho1p through Phosphorylation of RhoGEF Tus1p in Saccharomyces cerevisiae

Keiko Kono,*{dagger} Satoru Nogami,* Mitsuhiro Abe,* Masafumi Nishizawa,{ddagger} Shinichi Morishita,{sect} David Pellman,{dagger} and Yoshikazu Ohya*

*Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan; {dagger}Department of Pediatric Oncology, Dana-Farber Cancer Institute and Division of Hematology/Oncology, Children’s Hospital Boston and Harvard Medical School, Boston, MA 02115; {ddagger}Department of Microbiology and Immunology, Keio University School of Medicine, Tokyo 160-8582, Japan; {sect}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.


Address correspondence to: Yoshikazu Ohya (ohya{at}k.u-tokyo.ac.jp)




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