Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism
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Binding Sites
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CDC28 Protein Kinase, S cerevisiae / genetics
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CDC28 Protein Kinase, S cerevisiae / metabolism
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Cell Division
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Cyclin-Dependent Kinases / genetics
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Cyclin-Dependent Kinases / metabolism*
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Cyclins / genetics
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Cyclins / metabolism
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Enzyme Activation
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G1 Phase
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Genes, Fungal
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Guanine Nucleotide Exchange Factors / genetics
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Guanine Nucleotide Exchange Factors / metabolism*
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Models, Biological
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Mutation
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Phosphorylation
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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S Phase
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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rho GTP-Binding Proteins / genetics
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rho GTP-Binding Proteins / metabolism*
Substances
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Actins
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CLN2 protein, S cerevisiae
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Cyclins
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Guanine Nucleotide Exchange Factors
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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TUS1 protein, S cerevisiae
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CDC28 Protein Kinase, S cerevisiae
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Cyclin-Dependent Kinases
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RHO1 protein, S cerevisiae
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rho GTP-Binding Proteins