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Science 15 March 1996:
Vol. 271. no. 5255, pp. 1597 - 1601
DOI: 10.1126/science.271.5255.1597

Reports

Rapid Degradation of the G1 Cyclin Cln2 Induced by CDK-Dependent Phosphorylation

Stefan Lanker, M. Henar Valdivieso, Curt Wittenberg *

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.

S. Lanker and C. Wittenberg, Departments of Molecular Biology and Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
M. H. Valdivieso, Edificio Departamental, Microbiologia, Biologia, Avenida Del Campo Charro s/n, 37007 Salamanca, Spain.
* To whom correspondence should be addressed.



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