Journal
JOURNAL OF MOLECULAR CELL BIOLOGY
Volume 3, Issue 4, Pages 260-267Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jmcb/mjq037
Keywords
Aurora B; kinase sensor; phospho-CENP-A; PLK1; survivin
Categories
Funding
- National Institutes of Health (NIH) [DK-56292, CA132389]
- NIH
- National Center for Research Resources (NCRR) [UL1 RR025008]
- Chinese Natural Science Foundation [30500183, 30870990, 90508002, 90913016]
- Chinese Academy of Science [KSCX1-YW-R-65, KSCX2-YW-H-10, KSCX2-YW-R-195]
- Major State Basic Research Development Program of China (973 Program) [2007CB914503, 2010CB912103, 2009DFA31010, 2006BAI08B01-07]
- Georgia Cancer Coalition Breast Cancer Research Grant
- Atlanta Clinical and Translational Science Award Chemical Biology Grant [P20RR011104]
- Anhui Province Key Project [08040102005]
- NCRR, NIH [G12RR03034]
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During cell division, chromosome segregation is orchestrated by the interaction of spindle microtubules with the centromere. Accurate attachment of spindle microtubules to kinetochore requires the chromosomal passenger of Aurora B kinase complex with borealin, INCENP and survivin (SUR). The current working model argues that SUR is responsible for docking Aurora B to the centromere whereas its precise role in Aurora B activation has been unclear. Here, we show that Aurora B kinase activation requires SUR priming phosphorylation at Ser20 which is catalyzed by polo-like kinase 1 (PLK1). Inhibition of PLK1 kinase activity or expression of non-phosphorylatable SUR mutant prevents Aurora B activation and correct spindle microtubule attachment. The PLK1-mediated regulation of Aurora B kinase activity was examined in real-time mitosis using fluorescence resonance energy transfer-based reporter and quantitative analysis of native Aurora B substrate phosphorylation. We reason that the PLK1-mediated priming phosphorylation is critical for orchestrating Aurora B activity in centromere which is essential for accurate chromosome segregation and faithful completion of cytokinesis.
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