Orientation and structure of the Ndc80 complex on the microtubule lattice

Elizabeth M. Wilson-Kubalek, Iain M. Cheeseman, Craig Yoshioka, Arshad Desai, Ronald A. Milligan

Research output: Contribution to journalArticle

61 Scopus citations

Abstract

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 α/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.

Original languageEnglish (US)
Pages (from-to)1055-1061
Number of pages7
JournalJournal of Cell Biology
Volume182
Issue number6
DOIs
StatePublished - Sep 22 2008

ASJC Scopus subject areas

  • Cell Biology

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    Wilson-Kubalek, E. M., Cheeseman, I. M., Yoshioka, C., Desai, A., & Milligan, R. A. (2008). Orientation and structure of the Ndc80 complex on the microtubule lattice. Journal of Cell Biology, 182(6), 1055-1061. https://doi.org/10.1083/jcb.200804170