Aurora B kinase controls the targeting of the Astrin-SKAP complex to bioriented kinetochores
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Cheeseman_Aurora B kinase.pdf
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Author(s)
Schmidt, Jens Christopher
Kiyomitsu, Tomomi
Hori, Tetsuya
Backer, Chelsea B.
Fukagawa, Tatsuo
Cheeseman, Iain M
Date Issued
October 2010
Journal
Journal of Cell Biology
Publisher
Rockefeller University Press
Citation
Schmidt, J. C., T. Kiyomitsu, T. Hori, C. B. Backer, T. Fukagawa, and I. M. Cheeseman. “Aurora B kinase controls the targeting of the Astrin-SKAP complex to bioriented kinetochores.” Journal of Cell Biology 191, no. 2 (October 18, 2010): 269-280.
Version
Final published version
Abstract
During mitosis, kinetochores play multiple roles to generate interactions with microtubules, and direct chromosome congression, biorientation, error correction, and anaphase segregation. However, it is unclear what changes at the kinetochore facilitate these distinct activities. Here, we describe a complex of the spindle- and kinetochore-associated protein Astrin, the small kinetochore-associated protein (SKAP), and the dynein light chain LC8. Although most dynein-associated proteins localize to unaligned kinetochores in an Aurora B–dependent manner, Astrin, SKAP, and LC8 localization is antagonized by Aurora B such that they target exclusively to bioriented kinetochores. Astrin–SKAP-depleted cells fail to maintain proper chromosome alignment, resulting in a spindle assembly checkpoint–dependent mitotic delay. Consistent with a role in stabilizing bioriented attachments, Astrin and SKAP bind directly to microtubules and are required for CLASP localization to kinetochores. In total, our results suggest that tension-dependent Aurora B phosphorylation can act to control outer kinetochore composition to provide distinct activities to prometaphase and metaphase kinetochores.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1083/jcb.201006129
