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Control of Cyclin Ubiquitination by CDK-Regulated Binding of Hct1 to the Anaphase Promoting Complex

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Science  27 Nov 1998:
Vol. 282, Issue 5394, pp. 1721-1724
DOI: 10.1126/science.282.5394.1721

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Abstract

Proteolysis of mitotic cyclins depends on a multisubunit ubiquitin–protein ligase, the anaphase promoting complex (APC). Proteolysis commences during anaphase, persisting throughout G1 until it is terminated by cyclin-dependent kinases (CDKs) as cells enter S phase. Proteolysis of mitotic cyclins in yeast was shown to require association of the APC with the substrate-specific activator Hct1 (also called Cdh1). Phosphorylation of Hct1 by CDKs blocked the Hct1-APC interaction. The mutual inhibition between APC and CDKs explains how cells suppress mitotic CDK activity during G1 and then establish a period with elevated kinase activity from S phase until anaphase.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: wolfgang.seufert{at}po.uni-stuttgart.de

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