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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.

Type

Journal article

Journal

Science

Publication Date

27/11/1998

Volume

282

Pages

1721 - 1724

Keywords

Anaphase, Anaphase-Promoting Complex-Cyclosome, CDC2 Protein Kinase, Cdh1 Proteins, Cyclin-Dependent Kinases, Cyclins, Fungal Proteins, G1 Phase, Ligases, Mitosis, Phosphorylation, Recombinant Fusion Proteins, S Phase, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Protein Ligases, Ubiquitins