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Reference: Kono K, et al. (2008) G1/S Cyclin-dependent Kinase Regulates Small GTPase Rho1p through Phosphorylation of RhoGEF Tus1p in Saccharomyces cerevisiae. Mol Biol Cell 19(4):1763-1771

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Abstract

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.

Reference Type
Journal Article
Authors
Kono K, Nogami S, Abe M, Nishizawa M, Morishita S, Pellman D, Ohya Y
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