Role of the Ubiquitin-Proteasome Pathway in Regulating Abundance of the Cyclin-Dependent Kinase Inhibitor p27
Copyright policy )Role of the Ubiquitin-Proteasome Pathway in Regulating Abundance of the Cyclin-Dependent Kinase Inhibitor p27
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.
- University of Trieste Italy
- Wayne State College United States
- Hong Kong University of Science and Technology Hong Kong
- Hong Kong University of Science and Technology China (People's Republic of)
- GPC Biotech France
570, Proteasome Endopeptidase Complex, Leupeptins, 610, Cell Cycle Proteins, Anaphase-Promoting Complex-Cyclosome, Cyclin-Dependent Kinases, Recombinant Proteins, Cell Line, Ligases, Cysteine Endopeptidases, Kinetics, Mice, Adenosine Triphosphate, Electroporation, Multienzyme Complexes, Animals, Humans, Rabbits, Enzyme Inhibitors, Microtubule-Associated Proteins, Cyclin-Dependent Kinase Inhibitor p27
570, Proteasome Endopeptidase Complex, Leupeptins, 610, Cell Cycle Proteins, Anaphase-Promoting Complex-Cyclosome, Cyclin-Dependent Kinases, Recombinant Proteins, Cell Line, Ligases, Cysteine Endopeptidases, Kinetics, Mice, Adenosine Triphosphate, Electroporation, Multienzyme Complexes, Animals, Humans, Rabbits, Enzyme Inhibitors, Microtubule-Associated Proteins, Cyclin-Dependent Kinase Inhibitor p27
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