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The APC/C subunit Mnd2/Apc15 promotes Cdc20 autoubiquitination and spindle assembly checkpoint inactivation.

Molecular cell | Sep 28, 2012

http://www.ncbi.nlm.nih.gov/pubmed/22940250

The fidelity of chromosome segregation depends on the spindle assembly checkpoint (SAC). In the presence of unattached kinetochores, anaphase is delayed when three SAC components (Mad2, Mad3/BubR1, and Bub3) inhibit Cdc20, the activating subunit of the anaphase-promoting complex (APC/C). We analyzed the role of Cdc20 autoubiquitination in the SAC of budding yeast. Reconstitution with purified components revealed that a Mad3-Bub3 complex synergizes with Mad2 to lock Cdc20 on the APC/C and stimulate Cdc20 autoubiquitination, while inhibiting ubiquitination of substrates. SAC-dependent Cdc20 autoubiquitination required the Mnd2/Apc15 subunit of the APC/C. General inhibition of Cdc20 ubiquitination in vivo resulted in high Cdc20 levels and a failure to establish a SAC arrest, suggesting that SAC establishment depends on low Cdc20 levels. Specific inhibition of SAC-dependent ubiquitination, by deletion of Mnd2, allowed establishment of a SAC arrest but delayed release from the arrest, suggesting that Cdc20 ubiquitination is also required for SAC inactivation.

Pubmed ID: 22940250 RIS Download

Mesh terms: Anaphase-Promoting Complex-Cyclosome | Cdc20 Proteins | Cell Cycle Proteins | Chromosome Segregation | M Phase Cell Cycle Checkpoints | Mad2 Proteins | Nuclear Proteins | Saccharomyces cerevisiae Proteins | Spindle Apparatus | Ubiquitin-Protein Ligase Complexes | Ubiquitination

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM053270
  • Agency: NIGMS NIH HHS, Id: R37 GM053270

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