Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27

Michele Pagano, Sun W. Tam, Anne M. Theodoras, Peggy Beer-Romero, Giannino Del Sal, Vincent Chau, P. Renée Yew, Giulio F. Draetta, Mark Rolfe

Research output: Contribution to journalArticlepeer-review

1698 Scopus citations

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 languageEnglish (US)
Pages (from-to)682-685
Number of pages4
JournalScience
Volume269
Issue number5224
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

ASJC Scopus subject areas

  • General

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