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Borealin dimerization mediates optimal CPC checkpoint function by enhancing localization to centromeres and kinetochores

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  • Michael E. Bekier

    (University of Toledo
    Present address: Department of Molecular, Cellular and Developmental Biology, University of Michigan, 2127A Natural Science, 830 North University, Ann Arbor, Michigan 48109, USA)

  • Travis Mazur

    (University of Toledo)

  • Maisha S. Rashid

    (University of Toledo)

  • William R. Taylor

    (University of Toledo)

Abstract

The chromosomal passenger complex (CPC) localizes to centromeres where it activates the mitotic checkpoint in response to inappropriate inter-kinetochore tension. This error correction function is essential for proper chromosome segregation. Here we define several critical features of CPC localization and function. First, the Borealin dimerization domain suppresses dynamic exchange at the centromere to allow optimal CPC function. Second, Borealin dimerization is essential to target a subpopulation of CPC proximal to the kinetochore when the mitotic spindle is disrupted. This subpopulation is also needed for full CPC checkpoint function. The existence of a pool of CPC at the kinetochore suggests that error correction is more complicated than predicted from the Aurora B phosphorylation gradient model. Finally, Haspin kinase plays a key role in maintaining the slowly exchanging centromere Borealin pool, while Aurora B and Mps1 play minimal roles in maintaining CPC localization once cells are in mitosis.

Suggested Citation

  • Michael E. Bekier & Travis Mazur & Maisha S. Rashid & William R. Taylor, 2015. "Borealin dimerization mediates optimal CPC checkpoint function by enhancing localization to centromeres and kinetochores," Nature Communications, Nature, vol. 6(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7775
    DOI: 10.1038/ncomms7775
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