Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex.
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.
Mesh Terms:
Anaphase, CDC2 Protein Kinase, 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
Anaphase, CDC2 Protein Kinase, 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
Science
Date: Nov. 27, 1998
PubMed ID: 9831566
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