ROLE OF THE UBIQUITIN-PROTEASOME PATHWAY IN REGULATING ABUNDANCE OF THE CYCLIN-DEPENDENT KINASE INHIBITOR P27

被引：1721
作者：
PAGANO, M
TAM, SW
THEODORAS, AM
BEERROMERO, P
DELSAL, G
CHAU, V
YEW, PR
DRAETTA, GF
ROLFE, M
机构：
[1] WAYNE STATE UNIV, DEPT PHARMACOL, DETROIT, MI 48201 USA
[2] HARVARD UNIV, SCH MED, DEPT CELL BIOL, BOSTON, MA 02115 USA
来源：
SCIENCE | 1995年 / 269卷 / 5224期
关键词：
D O I：
10.1126/science.7624798
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
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页码：682 / 685
页数：4
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