Journal
NATURE CELL BIOLOGY
Volume 17, Issue 4, Pages 421-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb3128
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Funding
- Wellcome Trust [096535, 083524, 097945]
- Medical Research Council [84678]
- EC FP7 MitoSys [241548]
- ERC advanced grant [322682]
- Cancer Research UK [A6996]
- Human Frontier Science Program [RGP0035-2009]
- BBSRC
- European Research Council (ERC) [322682] Funding Source: European Research Council (ERC)
- Medical Research Council [G0701147] Funding Source: researchfish
- Wellcome Trust [096535/Z/11/Z] Funding Source: researchfish
- MRC [G0701147] Funding Source: UKRI
- Wellcome Trust [096535/Z/11/Z] Funding Source: Wellcome Trust
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For proper chromosome segregation, sister kinetochores must interact with microtubules from opposite spindle poles (bi-orientation). To establish bi-orientation, aberrant kinetochore-microtubule attachments are disrupted (error correction) by aurora B kinase (Ipl1 in budding yeast). Paradoxically, during this disruption, new attachments are still formed efficiently to enable fresh attempts at bi-orientation. How this is possible remains an enigma. Here we show that kinetochore attachment to the microtubule lattice (lateral attachment) is impervious to aurora B regulation, but attachment to the microtubule plus end (end-on attachment) is disrupted by this kinase. Thus, a new lateral attachment is formed without interference, then converted to end-on attachment and released if incorrect. This process continues until bi-orientation is established and stabilized by tension across sister kinetochores. We reveal how aurora B specifically promotes disruption of the end-on attachment through phospho-regulation of kinetochore components Dam1 and Ndc80. Our results reveal fundamental mechanisms for promoting error correction for bi-orientation.
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