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Originally published In Press as doi:10.1074/jbc.M107087200 on August 29, 2001

J. Biol. Chem., Vol. 276, Issue 45, 41725-41732, November 9, 2001
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A Cdc28 Mutant Uncouples G1 Cyclin Phosphorylation and Ubiquitination from G1 Cyclin Proteolysis*

Elena CeccarelliDagger and Carl Mann§

From the Service de Biochimie et de Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette, Cedex, France

Proteolysis of the yeast G1 cyclins is triggered by their Cdc28-dependent phosphorylation. Phosphorylated Cln1 and Cln2 are ubiquitinated by the SCF-Grr1 complex and then degraded by the 26 S proteasome. In this study, we identified a cak1 allele in a genetic screen for mutants that stabilize the yeast G1 cyclins. Further characterization showed that Cln2HA was hypophosphorylated, unable to bind Cdc28, and stabilized in cak1 mutants at the restrictive temperature. Hypophosphorylation of Cln2HA could thus explain its stabilization. To test this possibility, we expressed a Cak1-independent mutant of Cdc28 (Cdc28-43244) in cak1 mutants and found that Cln2HA phosphorylation was restored, but surprisingly, the phospho-Cln2HA was stabilized. When bound to Cdc28-43244, Cln2HA was recognized and polyubiquitinated by SCF-Grr1. The Cdc28-43244 mutant thus reveals an unexpected complexity in the degradation of polyubiquitinated Cln2HA by the proteasome.

* This work was supported in part by a European Union BioMed 2 network.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

This is dedicated to Elisa and Billie.

Dagger Supported by Postdoctoral Research Fellowship Contract ERBFMBICT 972209 from the European Union.

§ To whom correspondence should be addressed. Tel.: 33-1-69 08 34 32; Fax: 33-1-69 08 47 12; E-mail: mann@jonas.saclay.cea.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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