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.

引用

页码：682 / 685

页数：4

共 34 条

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