Catalytic assembly of the mitotic checkpoint inhibitor BubR1-Cdc20 by a Mad2-induced functional switch in Cdc20.

@article{Han2013CatalyticAO,
  title={Catalytic assembly of the mitotic checkpoint inhibitor BubR1-Cdc20 by a Mad2-induced functional switch in Cdc20.},
  author={Joo Seok Han and Andrew J Holland and Daniele Fachinetti and Anita Kulukian and Bulent Cetin and Don W Cleveland},
  journal={Molecular cell},
  year={2013},
  volume={51 1},
  pages={92-104}
}
The mitotic checkpoint acts to maintain chromosome content by generation of a diffusible anaphase inhibitor. Unattached kinetochores catalyze a conformational shift in Mad2, converting an inactive open form into a closed form that can capture Cdc20, the mitotic activator of the APC/C ubiquitin ligase. Mad2 binding is now shown to promote a functional switch in Cdc20, exposing a previously inaccessible site for binding to BubR1's conserved Mad3 homology domain. BubR1, but not Mad2, binding to… CONTINUE READING
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p31comet Promotes disassembly of the mitotic checkpoint complex in an ATP-dependent process.

Proceedings of the National Academy of Sciences of the United States of America • 2011
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