Abstract
Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G 1 cyclins are essential, rate-limiting activators of cell cycle initiation. G 1 -specific accumulation of one G 1 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.
References
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Dates
Type | When |
---|---|
Created | 18 years, 9 months ago (Oct. 27, 2006, 2:30 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 4:25 p.m.) |
Indexed | 1 month, 1 week ago (July 14, 2025, 11:45 p.m.) |
Issued | 29 years, 5 months ago (March 15, 1996) |
Published | 29 years, 5 months ago (March 15, 1996) |
Published Print | 29 years, 5 months ago (March 15, 1996) |
@article{Lanker_1996, title={Rapid Degradation of the G 1 Cyclin Cln2 Induced by CDK-Dependent Phosphorylation}, volume={271}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.271.5255.1597}, DOI={10.1126/science.271.5255.1597}, number={5255}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Lanker, Stefan and Valdivieso, M. Henar and Wittenberg, Curt}, year={1996}, month=mar, pages={1597–1601} }