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Published online
doi:10.1083/jcb.200804170
The Journal of Cell Biology, Vol. 182, No. 6, 1055-1061
The Rockefeller University Press, 0021-9525 $30.00
© Wilson-Kubalek et al.
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Orientation and structure of the Ndc80 complex on the microtubule lattice



Elizabeth M. Wilson-Kubalek1, Iain M. Cheeseman2,3, Craig Yoshioka1, Arshad Desai2,3, and Ronald A. Milligan1

1 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
2 Ludwig Institute for Cancer Research and 3 Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093

Correspondence to Arshad Desai: abdesai{at}ucsd.edu; or Ronald A. Milligan: milligan{at}scripps.edu

The four-subunit Ndc80 complex, comprised of Ndc80/Nuf2 and Spc24/Spc25 dimers, directly connects kinetochores to spindle microtubules. The complex is anchored to the kinetochore at the Spc24/25 end, and the Ndc80/Nuf2 dimer projects outward to bind to microtubules. Here, we use cryoelectron microscopy and helical image analysis to visualize the interaction of the Ndc80/Nuf2 dimer with microtubules. Our results, when combined with crystallography data, suggest that the globular domain of the Ndc80 subunit binds strongly at the interface between tubulin dimers and weakly at the adjacent intradimer interface along the protofilament axis. Such a binding mode, in which the Ndc80 complex interacts with sequential {alpha}/β-tubulin heterodimers, may be important for stabilizing kinetochore-bound microtubules. Additionally, we define the binding of the Ndc80 complex relative to microtubule polarity, which reveals that the microtubule interaction surface is at a considerable distance from the opposite kinetochore-anchored end; this binding geometry may facilitate polymerization and depolymerization at kinetochore-attached microtubule ends.

I.M. Cheeseman's present address is Whitehead Institute for Biomedical Research and Dept. of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142.

Abbreviation used in this paper: CH, calponin homology.

© 2008 Wilson-Kubalek et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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