Cdc53 Targets Phosphorylated G1 Cyclins for Degradation by the Ubiquitin Proteolytic Pathway
| Autor: | E.Elizabeth Patton, Neal Mathias, Mike Tyers, Timothy F Nason, Andrew Willems, Karen L Craig, Curt Wittenberg, Stefan Lanker, Ryuji Kobayashi |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Saccharomyces cerevisiae Proteins
Cell division Ubiquitin-Protein Ligases Molecular Sequence Data Cell Cycle Proteins Ubiquitin-conjugating enzyme General Biochemistry Genetics and Molecular Biology Anaphase-Promoting Complex-Cyclosome APC/C activator protein CDH1 Cell Line Fungal Proteins Ligases Cyclin-dependent kinase Cyclins Cell division control protein 4 Amino Acid Sequence Phosphorylation Ubiquitins Cyclin-dependent kinase 1 biology Biochemistry Genetics and Molecular Biology(all) G1 Phase Ubiquitin-Protein Ligase Complexes Cullin Proteins Sic1 Cyclin-Dependent Kinases Ubiquitin ligase Cell biology Enzyme Activation Biochemistry Mutation Ubiquitin-Conjugating Enzymes biology.protein Electrophoresis Polyacrylamide Gel Plasmids |
| Zdroj: | Cell. (3):453-463 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/S0092-8674(00)80118-X |
| Popis: | In budding yeast, cell division is initiated in late G1 phase once the Cdc28 cyclin-dependent kinase is activated by the G1 cyclins Cln1, Cln2, and Cln3. The extreme instability of the Cln proteins couples environmental signals, which regulate Cln synthesis, to cell division. We isolated Cdc53 as a Cln2-associated protein and show that Cdc53 is required for Cln2 instability and ubiquitination in vivo. The Cln2–Cdc53 interaction, Cln2 ubiquitination, and Cln2 instability all depend on phosphorylation of Cln2. Cdc53 also binds the E2 ubiquitin-conjugating enzyme, Cdc34. These findings suggest that Cdc53 is a component of a ubiquitin–protein ligase complex that targets phosphorylated G1 cyclins for degradation by the ubiquitin–proteasome pathway. |
| Databáze: | OpenAIRE |
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