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  Cyclin A2 degradation during the spindle assembly checkpoint requires multiple binding modes to the APC/C

Zhang, S., Tischer, T., & Barford, D. (2019). Cyclin A2 degradation during the spindle assembly checkpoint requires multiple binding modes to the APC/C. Nature Communications, 10: 3863. doi:10.1038/s41467-019-11833-2.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-AB15-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0004-AB20-7
Genre: Journal Article

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 Creators:
Zhang, S.1, Author              
Tischer, T., Author
Barford, D., Author
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: The anaphase-promoting complex/cyclosome (APC/C) orchestrates cell cycle progression by controlling the temporal degradation of specific cell cycle regulators. Although cyclin A2 and cyclin B1 are both targeted for degradation by the APC/C, during the spindle assembly checkpoint (SAC), the mitotic checkpoint complex (MCC) represses APC/C's activity towards cyclin B1, but not cyclin A2. Through structural, biochemical and in vivo analysis, we identify a non-canonical D box (D2) that is critical for cyclin A2 ubiquitination in vitro and degradation in vivo. During the SAC, cyclin A2 is ubiquitinated by the repressed APC/C-MCC, mediated by the cooperative engagement of its KEN and D2 boxes, ABBA motif, and the cofactor Cks. Once the SAC is satisfied, cyclin A2 binds APC/C-Cdc20 through two mutually exclusive binding modes, resulting in differential ubiquitination efficiency. Our findings reveal that a single substrate can engage an E3 ligase through multiple binding modes, affecting its degradation timing and efficiency.

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Language(s): eng - English
 Dates: 2019-08-29
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-019-11833-2
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Title: Nature Communications
Source Genre: Journal
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Pages: 16 Volume / Issue: 10 Sequence Number: 3863 Start / End Page: - Identifier: -