Role of the Ubiquitin-Proteasome Pathway in Regulating Abundance of the Cyclin-Dependent Kinase Inhibitor p27
| Autor: | Vincent Chau, Peggy Beer-Romero, Anne M. Theodoras, Sun W. Tam, Giulio Draetta, Michele Pagano, Mark Rolfe, Giannino Del Sal, P. Renee Yew |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Proteasome Endopeptidase Complex
Leupeptins Ubiquitin-Protein Ligases Proteolysis Cell Cycle Proteins Anaphase-Promoting Complex-Cyclosome Cell Line Ligases Mice Adenosine Triphosphate Ubiquitin Multienzyme Complexes Tumor Cells Cultured medicine SKP2 Animals Humans Enzyme Inhibitors Protein kinase A Ubiquitins Cyclin Multidisciplinary medicine.diagnostic_test biology Kinase Tumor Suppressor Proteins Ubiquitin-Protein Ligase Complexes Succinates Cell cycle Cyclin-Dependent Kinases Recombinant Proteins Cell biology Cysteine Endopeptidases Kinetics Electroporation Biochemistry Proteasome Ubiquitin-Conjugating Enzymes biology.protein Rabbits Microtubule-Associated Proteins Cyclin-Dependent Kinase Inhibitor p27 |
| Zdroj: | Science. 269:682-685 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | The p27 mammalian cell cycle protein is an inhibitor of cyclin-dependent kinases. Both in vivo and in vitro, p27 was found to be degraded by the ubiquitin-proteasome pathway. The human ubiquitin-conjugating enzymes Ubc2 and Ubc3 were specifically involved in the ubiquitination of p27. Compared with proliferating cells, quiescent cells exhibited a smaller amount of p27 ubiquitinating activity, which accounted for the marked increase of p27 half-life measured in these cells. Thus, the abundance of p27 in cells is regulated by degradation. The specific proteolysis of p27 may represent a mechanism for regulating the activity of cyclin-dependent kinases. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|