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Title

Cdk1 Phosphorylates SPAT-1/Bora to Promote Plk1 Activation in C. elegans and Human Cells

Authors
Thomas, Yann
Martino, Lisa
Tavernier, Nicolas
Van Hove, Lucie
Joly, Nicolas
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Published in Cell Reports. 2016, vol. 15, no. 3, p. 510-8
Abstract The conserved Bora protein is a Plk1 activator, essential for checkpoint recovery after DNA damage in human cells. Here, we show that Bora interacts with Cyclin B and is phosphorylated by Cyclin B/Cdk1 at several sites. The first 225 amino acids of Bora, which contain two Cyclin binding sites and three conserved phosphorylated residues, are sufficient to promote Plk1 phosphorylation by Aurora A in vitro. Mutating the Cyclin binding sites or the three conserved phosphorylation sites abrogates the ability of the N terminus of Bora to promote Plk1 activation. In human cells, Bora-carrying mutations of the three conserved phosphorylation sites cannot sustain mitotic entry after DNA damage. In C. elegans embryos, mutation of the three conserved phosphorylation sites in SPAT-1, the Bora ortholog, results in a severe mitotic entry delay. Our results reveal a crucial and conserved role of phosphorylation of the N terminus of Bora for Plk1 activation and mitotic entry.
Identifiers
PMID: 27068477
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Structures
Research group La division asymétrique (847)
Project FNS: 31003A 156013
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(ISO format)
THOMAS, Yann et al. Cdk1 Phosphorylates SPAT-1/Bora to Promote Plk1 Activation in C. elegans and Human Cells. In: Cell Reports, 2016, vol. 15, n° 3, p. 510-8. https://archive-ouverte.unige.ch/unige:84661

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Deposited on : 2016-06-20

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