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...

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Bibliographic Details

Published in:	Genes Dev
Main Authors:	Montagnoli, Alessia, Fiore, Francesca, Eytan, Esther, Carrano, Andrea C., Draetta, Giulio F., Hershko, Avram, Pagano, Michele
Format:	Artigo
Language:	Inglês
Published:	Cold Spring Harbor Laboratory Press 1999
Subjects:	Research Paper
Online Access:	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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