Liu Dan, Vader Gerben, Vromans Martijn J M, Lampson Michael A, Lens Susanne M A
Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Science. 2009 Mar 6;323(5919):1350-3. doi: 10.1126/science.1167000. Epub 2009 Jan 15.
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.
成功的细胞分裂需要染色体附着于有丝分裂纺锤体的相对两极(双定向)。Aurora B激酶通过磷酸化与微管结合的动粒底物来调节染色体与纺锤体的附着。着丝粒张力可稳定双定向附着,但物理力如何在单个着丝粒处转化为信号尚不清楚。我们使用基于荧光共振能量转移的生物传感器来测量活细胞中的局部磷酸化动力学,发现动粒处Aurora B底物的磷酸化取决于其与着丝粒内部激酶的距离。此外,将Aurora B重新定位到更靠近动粒的位置会阻止双定向附着的稳定并激活纺锤体检查点。因此,着丝粒张力可通过Aurora B与动粒底物空间距离的增加来感知,这会减少磷酸化并稳定动粒微管。