Rapid Degradation of the G 1 Cyclin Cln2 Induced by CDK-Dependent Phosphorylation

Abstract

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.