Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
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.

Bibliography

Lanker, S., Valdivieso, M. H., & Wittenberg, C. (1996). Rapid Degradation of the G 1 Cyclin Cln2 Induced by CDK-Dependent Phosphorylation. Science, 271(5255), 1597–1601.

Authors 3
  1. Stefan Lanker (first)
  2. M. Henar Valdivieso (additional)
  3. Curt Wittenberg (additional)
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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)
Funders 0

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@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} }