| | |  | | | | Record from Web of Science® | | | | | | |
| ROLE OF THE UBIQUITIN-PROTEASOME PATHWAY IN REGULATING ABUNDANCE OF THE CYCLIN-DEPENDENT KINASE INHIBITOR P27 |
|
|
| Author(s): PAGANO M, TAM SW, THEODORAS AM, BEERROMERO P, DELSAL G, CHAU V, YEW PR, DRAETTA GF, ROLFE M |
| Source: SCIENCE Volume: 269 Issue: 5224 Pages: 682-685 Published: AUG 4 1995 |
| Times Cited: 1,395 References: 35 |
| 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: PAGANO, M (reprint author), MITOTIX INC, 1 KENDALL SQ, BLDG 600, CAMBRIDGE, MA 02139 USA |
Addresses:
1. WAYNE STATE UNIV, DEPT PHARMACOL, DETROIT, MI 48201 USA
2. HARVARD UNIV, SCH MED, DEPT CELL BIOL, BOSTON, MA 02115 USA |
| Publisher: AMER ASSOC ADVAN SCIENCE, 1333 H ST NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: RM702 |
| ISSN: 0036-8075 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |