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  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., 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.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-0F01-D Version Permalink: http://hdl.handle.net/21.11116/0000-0002-0F05-9
Genre: Journal Article

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2640473.pdf (Publisher version), 590KB
 
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Herzog, F., Author
Primorac, I., Author
Dube, P., Author
Lenart, P.1, Author              
Sander, B., Author
Mechtler, K., Author
Stark, H., Author
Peters, J. M., Author
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1Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society, ou_2640691              

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 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.

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Language(s): eng - English
 Dates: 2009-03-13
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.1163300
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 323 (5920) Sequence Number: - Start / End Page: 1477 - 1481 Identifier: -