Abstract
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.
Original language | English (US) |
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Pages (from-to) | 682-685 |
Number of pages | 4 |
Journal | Science |
Volume | 269 |
Issue number | 5224 |
DOIs | |
State | Published - 1995 |
All Science Journal Classification (ASJC) codes
- General