Ubiquitination of Cdc20 by the APC Occurs through an Intramolecular Mechanism

作者: Ian T. Foe , Scott A. Foster , Stephanie K. Cheung , Steven Z. DeLuca , David O. Morgan

DOI: 10.1016/J.CUB.2011.09.051

关键词: Cell cycleBiochemistryAPC/C activator protein CDH1UbiquitinBiologyCell biologyAnaphaseCDC20Saccharomyces cerevisiaeMitosisCell Cycle Protein

摘要: Summary Background Cells control progression through late mitosis by regulating Cdc20 and Cdh1, the two mitotic activators of anaphase-promoting complex (APC). The protein levels during cell cycle is not well understood. Results Here, we demonstrate that degraded in budding yeast multiple APC-dependent mechanisms. We find majority turnover does involve a second activator molecule but instead depends on cis autoubiquitination while it bound to its activator-binding site APC core. Unlike trans ubiquitination substrates, ubiquitinates independent activation Cdc20's C box. this intramolecular mechanism regulated, contributing decline occurs after anaphase. Interestingly, high substrate in vitro significantly reduce autoubiquitination. Conclusion show here fluctuates via a distinct form APC-mediated ubiquitination. This may preferentially occur early anaphase, following depletion substrates. suggests mechanisms are able target for at different points cycle.

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