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The ubiquitin ligase CRL2ZYG11 targets cyclin B1 for degradation in a conserved pathway that facilitates mitotic slippage.*

Posted by on in 2016
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Balachandran RS1Heighington CS2Starostina NG1Anderson JW1Owen DL1Vasudevan S1Kipreos ET3. 2016. J Cell Biol. 215(2):151-166. Epub 2016 Oct 17.

1Department of Cellular Biology, University of Georgia, Athens, GA 30602.
2Department of Genetics, University of Georgia, Athens, GA 30602.
3Department of Cellular Biology, University of Georgia, Athens, GA 30602 ekipreos@uga.edu.

Abstract

The anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase is known to target the degradation of cyclin B1, which is crucial for mitotic progression in animal cells. In this study, we show that the ubiquitin ligase CRL2ZYG-11 redundantly targets the degradation of cyclin B1 in Caenorhabditis elegans and human cells. In C. elegans, both CRL2ZYG-11 and APC/C are required for proper progression through meiotic divisions. In human cells, inactivation of CRL2ZYG11A/B has minimal effects on mitotic progression when APC/C is active. However, when APC/C is inactivated or cyclin B1 is overexpressed, CRL2ZYG11A/B-mediated degradation of cyclin B1 is required for normal progression through metaphase. Mitotic cells arrested by the spindle assembly checkpoint, which inactivates APC/C, often exit mitosis in a process termed "mitotic slippage," which generates tetraploid cells and limits the effectiveness of antimitotic chemotherapy drugs. We show that ZYG11A/B subunit knockdown, or broad cullin-RING ubiquitin ligase inactivation with the small molecule MLN4924, inhibits mitotic slippage in human cells, suggesting the potential for antimitotic combination therapy.

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PMID:
 
27810909
 
PMCID:
 
PMC5084644
 [Available on 2017-04-24]
 
DOI:
 
10.1083/jcb.201601083
[PubMed - in process]
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