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Dev Cell. 2015 Feb 9;32(3):358-72. doi: 10.1016/j.devcel.2015.01.003.

The ABBA motif binds APC/C activators and is shared by APC/C substrates and regulators.

Author information

1
The Gurdon Institute and Department of Zoology, University of Cambridge, Cambridge CB2 1QN, UK.
2
Department of Physiology and Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA; Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, 69117 Baden-Württemberg, Germany.
3
Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany.
4
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, 69117 Baden-Württemberg, Germany.
5
The Gurdon Institute and Department of Zoology, University of Cambridge, Cambridge CB2 1QN, UK. Electronic address: jp103@cam.ac.uk.

Abstract

The anaphase-promoting complex or cyclosome (APC/C) is the ubiquitin ligase that regulates mitosis by targeting specific proteins for degradation at specific times under the control of the spindle assembly checkpoint (SAC). How the APC/C recognizes its different substrates is a key problem in the control of cell division. Here, we have identified the ABBA motif in cyclin A, BUBR1, BUB1, and Acm1, and we show that it binds to the APC/C coactivator CDC20. The ABBA motif in cyclin A is required for its proper degradation in prometaphase through competing with BUBR1 for the same site on CDC20. Moreover, the ABBA motifs in BUBR1 and BUB1 are necessary for the SAC to work at full strength and to recruit CDC20 to kinetochores. Thus, we have identified a conserved motif integral to the proper control of mitosis that connects APC/C substrate recognition with the SAC.

PMID:
25669885
PMCID:
PMC4713905
DOI:
10.1016/j.devcel.2015.01.003
[Indexed for MEDLINE]
Free PMC Article
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