期刊
CELL REPORTS
卷 15, 期 3, 页码 510-518出版社
CELL PRESS
DOI: 10.1016/j.celrep.2016.03.049
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资金
- Miguel Servet program from the Instituto Carlos III (Spanish Ministry of Economy and Competitivity) [CP13/00158]
- Labex Who am I''? Laboratory of Excellence [ANR-11-LABX-0071]
- French Government through its Investments for the Future program
- Foundation for Medical Research
- ANR [ANR-2012-BSV2-0001-01]
- University of Geneva
- Swiss National Science Foundation [31003A_156013]
- NCCR Chemical Biology
- Foundation for Medical Research Equipe FRM [DEQ20140329538]
- French National Research Agency (ANR) [ANR-11-IDEX-0005-01]
- Swiss National Science Foundation (SNF) [31003A_156013] Funding Source: Swiss National Science Foundation (SNF)
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.
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