Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation.
Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G1 cyclins are essential, rate-limiting activators of cell cycle initiation. G1-specific accumulation of one G1 cyclin, Cln2, results from periodic gene expression coupled with rapid protein turnover. Site-directed mutagenesis of CLN2 revealed ... that its phosphorylation provides a signal that promotes rapid degradation. Cln2 phosphorylation is dependent on the Cdc28 protein kinase, the CDK that it activates. These findings suggest that Cln2 is rendered self-limiting by virtue of its ability to activate its cognate CDK subunit.
Mesh Terms:
Amino Acid Sequence, CDC28 Protein Kinase, S cerevisiae, Cyclins, Enzyme Activation, Fungal Proteins, G1 Phase, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Phenotype, Phosphorylation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Amino Acid Sequence, CDC28 Protein Kinase, S cerevisiae, Cyclins, Enzyme Activation, Fungal Proteins, G1 Phase, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Phenotype, Phosphorylation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Science
Date: Mar. 15, 1996
PubMed ID: 8599119
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