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    Science. 1998 Nov 27;282(5394):1721-4.

    Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex.

    Zachariae W, Schwab M, Nasmyth K, Seufert W.

    Source

    Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria.

    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.

    PMID:
    9831566
    [PubMed - indexed for MEDLINE]

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