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Cyclin destruction in mitosis: a crucial task of Cdc20
ISSN
0014-5793
Date Issued
2002
Author(s)
DOI
10.1016/S0014-5793(02)03657-8
Abstract
Proteolytic destruction of cyclins is a fundamental process for cell division. At the end of mitosis, degradation of mitotic cyclins results in the inactivation of cyclin-dependent kinases. Cyclin proteolysis is triggered by the anaphase-promoting complex/cyclosome (APC/C), a multi-subunit complex which contains ubiquitin ligase activity. Recent data in yeast demonstrated that a partial degradation of the mitotic cyclin Clb2, mediated by APC/C and its activator protein Cdc20, is essential and sufficient for the mitotic exit. Remarkably, a complete inactivation of cyclin-dependent kinases seems to be not essential. This review discusses recent novel insights into cyclin destruction and its implications for the mitotic exit. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.