Structural comparison of the Caenorhabditis elegans and human Ndc80 complexes bound to microtubules reveals distinct binding behavior
Name
Wilson-Kubalek-2016-Structural compariso.pdf
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1.59 MB
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Author(s)
Wilson-Kubalek, Elizabeth M.
Milligan, Ronald A.
Cheeseman, Iain M
Date Issued
March 2016
Journal
Molecular Biology of the Cell
Publisher
American Society for Cell Biology
Citation
Wilson-Kubalek, E. M., I. M. Cheeseman, and R. A. Milligan. “Structural Comparison of the Caenorhabditis Elegans and Human Ndc80 Complexes Bound to Microtubules Reveals Distinct Binding Behavior.” Molecular Biology of the Cell 27, no. 8 (April 15, 2016): 1197–1203.
Version
Final published version
Abstract
During cell division, kinetochores must remain tethered to the plus ends of dynamic microtubule polymers. However, the molecular basis for robust kinetochore–microtubule interactions remains poorly understood. The conserved four-subunit Ndc80 complex plays an essential and direct role in generating dynamic kinetochore–microtubule attachments. Here we compare the binding of the Caenorhabditis elegans and human Ndc80 complexes to microtubules at high resolution using cryo–electron microscopy reconstructions. Despite the conserved roles of the Ndc80 complex in diverse organisms, we find that the attachment mode of these complexes for microtubules is distinct. The human Ndc80 complex binds every tubulin monomer along the microtubule protofilament, whereas the C. elegans Ndc80 complex binds more tightly to β-tubulin. In addition, the C. elegans Ndc80 complex tilts more toward the adjacent protofilament. These structural differences in the Ndc80 complex between different species may play significant roles in the nature of kinetochore–microtubule interactions.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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DOI of Published Version
https://doi.org/10.1091/mbc.E15-12-0858
