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Vol. 12, No. 5, pp. 692-705, March 1, 1998
1 Programme in Molecular Biology and Cancer, Samuel
Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Canada M5G
1X5;
2 Graduate Department of Molecular and Medical Genetics,
University of Toronto, Toronto, Canada M5S 1A8;
3 Centre de
Genetique Moleculaire, Centre National de la Recherche Scientifique,
91198 Gif-sur-Yvette, France
In budding yeast, ubiquitination of the cyclin-dependent kinase
(Cdk) inhibitor Sic1 is catalyzed by the E2 ubiquitin conjugating enzyme Cdc34 in conjunction with an E3 ubiquitin ligase complex composed of Skp1, Cdc53 and the
F-box protein, Cdc4 (the SCFCdc4 complex). Skp1
binds a motif called the F-box and in turn F-box proteins appear to
recruit specific substrates for ubiquitination. We find that Skp1
interacts with Cdc53 in vivo, and that Skp1 bridges Cdc53 to three
different F-box proteins, Cdc4, Met30, and Grr1. Cdc53 contains
independent binding sites for Cdc34 and Skp1 suggesting it functions as
a scaffold protein within an E2/E3 core complex. F-box
proteins show remarkable functional specificity in vivo: Cdc4 is
specific for degradation of Sic1, Grr1 is specific for degradation of
the G1 cyclin Cln2, and Met30 is specific for repression of
methionine biosynthesis genes. In contrast, the Cdc34-Cdc53-Skp1
E2/E3 core complex is required for all three functions.
Combinatorial control of SCF complexes may provide a basis for the
regulation of diverse cellular processes.
[Key Words: SCF ubiquitin ligase; glucose; methionine; cyclin; Cdk; protein-protein interaction; Met30; Grrl; Cdc4]
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