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Originally published as MBC in Press, 10.1091/mbc.E07-09-0950 on February 6, 2008

Vol. 19, Issue 4, 1763-1771, April 2008

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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§, David Pellman{dagger}, and Yoshikazu Ohya*

Departments of *Integrated Biosciences and §Computational Biology, 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; and {ddagger}Department of Microbiology and Immunology, Keio University School of Medicine, Tokyo 160-8582, Japan

Submitted September 21, 2007; Revised January 16, 2008; Accepted January 30, 2008
Monitoring Editor: Mark Solomon

Rho1p is an essential small GTPase that plays a key role in the morphogenesis of Saccharomyces 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.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-09-0950) on February 6, 2008.

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




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