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| Content Provider | PubMed Central |
|---|---|
| Author | Singer, Jeffrey D. Mark, Gurian-west Clurman, Bruce Roberts, James M. |
| Copyright Year | 1999 |
| Abstract | Cyclin E is an unstable protein that is degraded in a ubiquitin- and proteasome- dependent pathway. Two factors stimulate cyclin E ubiquitination in vivo: when it is free of its CDK partner, and when it is phosphorylated on threonine 380. We pursued the first of these pathways by using a two-hybrid screen to identify proteins that could bind only to free cyclin E. This resulted in the isolation of human Cul-3, a member of the cullin family of E3 ubiquitin–protein ligases. We found that Cul-3 was bound to cyclin E but not to cyclin E-Cdk2 complexes in mammalian cells, and that overexpression of Cul-3 increased ubiquitination of cyclin E but not other cyclins. Conversely, deletion of the Cul-3 gene in mice caused increased accumulation of cyclin E protein, and had cell-type-specific effects on S-phase regulation. In the extraembryonic ectoderm, in which cells undergo a standard mitotic cycle, there was a greatly increased number of cells in S phase. In the trophectoderm, in which cells go through endocycles, there was a block to entry into S phase. The SCF pathway, which targets cyclins for ubiquitination on the basis of their phosphorylation state, and the Cul-3 pathway, which selects cyclin E for ubiquitination on the basis of its assembly into CDK complexes, may be complementary ways to control cyclin abundance. |
| Starting Page | 2375 |
| File Format | |
| ISSN | 08909369 |
| Journal | Genes & Development |
| Issue Number | 18 |
| Volume Number | 13 |
| Language | English |
| Publisher | Cold Spring Harbor Laboratory Press |
| Publisher Date | 1999-09-15 |
| Access Restriction | Open |
| Rights Holder | Cold Spring Harbor Laboratory Press |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Developmental Biology |
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