Cdc34 and the F-box protein Met30 are required for degradation of the Cdk-inhibitory kinase Swe1
| Autor: | Peter K. Kaiser, Daniel J. Lew, Steven I. Reed, Rey A. L. Sia, Elaine G.S. Bardes |
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| Rok vydání: | 1998 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Ubiquitin-Protein Ligases Protein subunit Molecular Sequence Data Mitosis Cell Cycle Proteins Saccharomyces cerevisiae Ubiquitin-conjugating enzyme medicine.disease_cause F-box protein Anaphase-Promoting Complex-Cyclosome Fungal Proteins Ligases Cyclin-dependent kinase Skp1 Genetics medicine Amino Acid Sequence Cell division control protein 4 Phosphorylation Cell Cycle Protein S-Phase Kinase-Associated Proteins Ubiquitins Mutation biology F-Box Proteins Cell Cycle Ubiquitin-Protein Ligase Complexes Protein-Tyrosine Kinases Cullin Proteins Repressor Proteins Enhancer Elements Genetic Biochemistry Ubiquitin-Conjugating Enzymes biology.protein Tyrosine Research Paper Developmental Biology |
| Zdroj: | Genes & Development. 12:2587-2597 |
| ISSN: | 1549-5477 0890-9369 |
| Popis: | Ubiquitin-mediated proteolysis controls the abundance of many cell cycle regulatory proteins. Recent work in Saccharomyces cerevisiae suggests that a complex consisting of Cdc53, Skp1, and a third component known as an F-box protein (termed SCF) in combination with Cdc34 specifically targets regulatory proteins for degradation, and that substrate specificity is likely to be mediated by the F-box subunit. A screen for genetic interactions with a cdc34mutation yielded MET30, which encodes an F-box protein.MET30 is an essential gene required for cell cycle progression and met30 mutations interact genetically with mutations in SCF components. Furthermore, physical interactions between Met30, Cdc53, Cdc34, and Skp1 in vivo provide evidence for an SCFMet30complex. We demonstrate the involvement of Met30 in the degradation of the Cdk-inhibitory kinase Swe1. Swe1 is stabilized in met30mutants and GST-Met30 pull-down experiments reveal that Met30 specifically binds Swe1 in vivo. Furthermore, extracts prepared fromcdc34 or met30 mutants are defective in polyubiquitination of Swe1. Taken together, these data suggest that SCF-mediated proteolysis may contribute to the regulation of entry into mitosis. Our data, in combination with previously published results, also provide evidence for distinct SCF complexes in vivo and support the idea that their F-box subunits mediate SCF substrate specificity. |
| Databáze: | OpenAIRE |
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