Structure of the anaphase-promoting complex/cyclosome interacting with a 
mitotic checkpoint complex.

Herzog, F.; Primorac, I.; Dube, P.; Lenart, P.; Sander, B.; Mechtler, K.; Stark, H.; Peters, J. M.

doi:10.1126/science.1163300

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Journal Article

Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex.

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Lenart, P.
Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Herzog, F., Primorac, I., Dube, P., Lenart, P., Sander, B., Mechtler, K., et al. (2009). Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex. Science, 323(5920), 1477-1481. doi:10.1126/science.1163300.

Cite as: https://hdl.handle.net/21.11116/0000-0002-0F01-D

Abstract

Once all chromosomes are connected to the mitotic spindle (bioriented), anaphase is initiated by the protein ubiquitylation activity of the anaphase-promoting complex/cyclosome (APC/C) and its coactivator Cdc20 (APC/C(Cdc20)). Before chromosome biorientation, anaphase is delayed by a mitotic checkpoint complex (MCC) that inhibits APC/C(Cdc20). We used single-particle electron microscopy to obtain three-dimensional models of human APC/C in various functional states: bound to MCC, to Cdc20, or to neither (apo-APC/C). These experiments revealed that MCC associates with the Cdc20 binding site on APC/C, locks the otherwise flexible APC/C in a "closed" state, and prevents binding and ubiquitylation of a wide range of different APC/C substrates. These observations clarify the structural basis for the inhibition of APC/C by spindle checkpoint proteins.