ROLE OF THE UBIQUITIN-PROTEASOME PATHWAY IN REGULATING ABUNDANCE OF THE CYCLIN-DEPENDENT KINASE INHIBITOR P27
ROLE OF THE UBIQUITIN-PROTEASOME PATHWAY IN REGULATING ABUNDANCE OF THE CYCLIN-DEPENDENT KINASE INHIBITOR P27
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DOI：
10.1126/science.7624798
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发表时间：
1995-08-04
期刊：
影响因子：
56.9
通讯作者：
ROLFE, M
中科院分区：
文献类型：
--
作者：
PAGANO, M;TAM, SW;ROLFE, M
p27哺乳动物细胞周期蛋白是细胞周期蛋白依赖性激酶的抑制剂。在体内和体外，p27被发现是由泛素-蛋白酶体途径降解。人泛素结合酶Ubc 2和Ubc 3特异性参与p27的泛素化。与增殖细胞相比，静止期细胞表现出较少量的p27泛素化活性，这是这些细胞中测得的p27半衰期显着增加的原因。因此，细胞中p27的丰度通过降解来调节。p27的特异性蛋白水解可能代表了调节细胞周期蛋白依赖性激酶活性的机制。
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.