Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
CELL cycle progression in eukaryotes is controlled by the p34cdc21CDC28 protein kinase and its Short-lived, phase-specific regulatory subunits called cyclins1,2. In Xenopus oocytes, degradation of M-phase (B-type) cyclins is required for exit from mitosis and is mediated by the ubiquitin-dependent p...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
05 January 1995
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| In: |
Nature
Year: 1995, Volume: 373, Issue: 6509, Pages: 78-81 |
| ISSN: | 1476-4687 |
| DOI: | 10.1038/373078a0 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/373078a0 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/373078a0 
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| Author Notes: | Wolfgang Seufert, Bruce Futcher, Stefan Jentsch |
| Summary: | CELL cycle progression in eukaryotes is controlled by the p34cdc21CDC28 protein kinase and its Short-lived, phase-specific regulatory subunits called cyclins1,2. In Xenopus oocytes, degradation of M-phase (B-type) cyclins is required for exit from mitosis and is mediated by the ubiquitin-dependent proteolytic system3. Here we show that B-type-cyclin degradation in yeast involves an essential nuclear ubiquitin-conjugating enzyme, UBC9. Repression of UBC9 synthesis prevents cell cycle progression at the G2 or early M phase, causing the accumulation of large budded cells with a single nucleus, a short spindle and replicated DNA. In ubc9 mutants both CLB5, an S-phase cyclin4,5, and CLB2, an M-phase cyclin6,7, are stabilized. In wild-type cells the CLB5 protein is unstable throughout the cell cycle, whereas CLB2 turnover occurs only at a specific cell-cycle stage8. Thus distinct degradation signals or regulated interaction with the ubiquitin-protein ligase system may determine the cell-cycle specificity of cyclin proteolysi |
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| Item Description: | Gesehen am 29.07.2026 |
| Physical Description: | Online Resource |
| ISSN: | 1476-4687 |
| DOI: | 10.1038/373078a0 |