Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
The cellular abundance of the cyclin-dependent kinase (Cdk) inhibitor p27 is regulated by the ubiquitin–proteasome system. Activation of p27 degradation is seen in proliferating cells and in many types of aggressive human carcinomas. p27 can be phosphorylated on threonine 187 by Cdks, and cyclin E/C...
Bewaard in:
| Gepubliceerd in: | Genes Dev |
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| Hoofdauteurs: | , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Cold Spring Harbor Laboratory Press
1999
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC316946/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10323868/ https://ncbi.nlm.nih.govhttps://doi.org/10.1101/gad.13.9.1181 |
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