Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 19, Issue 4, Pages 1763-1771Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E07-09-0950
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Funding
- Ministry of Education, Science, Sports, and Culture of Japan [16026205]
- Institute for Bioinformatics and Research and Development of the Japan Science and Technology Corporation
- Grants-in-Aid for Scientific Research [16026205] Funding Source: KAKEN
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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.
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