Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases.

TitleUbiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases.
Publication TypeJournal Article
Year of Publication1998
AuthorsZhou P, Howley PM
JournalMol Cell
Date Published1998 Nov
KeywordsAnaphase-Promoting Complex-Cyclosome, Carrier Proteins, CDC28 Protein Kinase, S cerevisiae, Cell Cycle, Cell Cycle Proteins, Cullin Proteins, Cyclins, Cysteine Endopeptidases, F-Box Proteins, Fungal Proteins, Half-Life, Hydroxyurea, Ligases, Lipoproteins, Multienzyme Complexes, Mutation, Nocodazole, Pheromones, Precipitin Tests, Proteasome Endopeptidase Complex, Recombinant Fusion Proteins, S-Phase Kinase-Associated Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Protein Ligases, Ubiquitins

The S. cerevisiae SCFCdc4p ubiquitin-protein ligase complex promotes cell cycle transitions through degradation of cell cycle regulators. To investigate SCFCdc4p regulation in vivo, we examined the stability of individual SCFCdc4p components. Whereas Cdc53p and Skp1p were stable, Cdc4p, the F box-containing component responsible for substrate recognition, was short lived and subject to SCF-mediated ubiquitination. Grr1p, another F box component of SCF complexes, was also ubiquitinated. A stable truncated Cdc4pF-beta-gal hybrid protein capable of binding Skp1p and entering into an SCF complex interfered with proteolysis of SCF targets and inhibited cell proliferation. The finding that the F box-containing SCF components are unstable suggests a mechanism of regulating SCF function through ubiquitination and proteolysis of F box components.

Alternate JournalMol Cell
PubMed ID9844630
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