Journal
SCIENCE
Volume 323, Issue 5919, Pages 1350-1353Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1167000
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Funding
- American Cancer Society [IRG-78-002-30]
- National Institutes of Health [GM083988]
- Searle Scholars Program
- Penn Genome Frontiers Institute
- Netherlands Organization for Scientific Research [Vidi 917.66.332]
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Successful cell division requires that chromosomes attach to opposite poles of the mitotic spindle (bi-orientation). Aurora B kinase regulates chromosome-spindle attachments by phosphorylating kinetochore substrates that bind microtubules. Centromere tension stabilizes bi-oriented attachments, but how physical forces are translated into signaling at individual centromeres is unknown. Using fluorescence resonance energy transfer-based biosensors to measure localized phosphorylation dynamics in living cells, we found that phosphorylation of an Aurora B substrate at the kinetochore depended on its distance from the kinase at the inner centromere. Furthermore, repositioning Aurora B closer to the kinetochore prevented stabilization of bi-oriented attachments and activated the spindle checkpoint. Thus, centromere tension can be sensed by increased spatial separation of Aurora B from kinetochore substrates, which reduces phosphorylation and stabilizes kinetochore microtubules.
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