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  • 1
    Publication Date: 1995-08-04
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pagano, M -- Tam, S W -- Theodoras, A M -- Beer-Romero, P -- Del Sal, G -- Chau, V -- Yew, P R -- Draetta, G F -- Rolfe, M -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):682-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mitotix Inc., Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624798" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Anaphase-Promoting Complex-Cyclosome ; Animals ; *Cell Cycle Proteins ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/*antagonists & inhibitors ; Cysteine Endopeptidases/*metabolism ; Electroporation ; Enzyme Inhibitors/metabolism ; Humans ; Kinetics ; Leupeptins/pharmacology ; Ligases/metabolism ; Mice ; Microtubule-Associated Proteins/*metabolism ; Multienzyme Complexes/*metabolism ; Proteasome Endopeptidase Complex ; Rabbits ; Recombinant Proteins/metabolism ; Succinates/pharmacology ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; Ubiquitin-Conjugating Enzymes ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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