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The Ndc80 kinetochore complex forms oligomeric arrays along microtubules

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  • Gregory M. Alushin

    (Biophysics Graduate Group, University of California)

  • Vincent H. Ramey

    (Biophysics Graduate Group, University of California)

  • Sebastiano Pasqualato

    (European Institute of Oncology)

  • David A. Ball

    (Lawrence Berkeley National Laboratory)

  • Nikolaus Grigorieff

    (Howard Hughes Medical Institute, Rosenstiel Basic Medical Research Center, Brandeis University)

  • Andrea Musacchio

    (European Institute of Oncology
    Research Unit of the Italian Institute of Technology at the IFOM-IEO Campus)

  • Eva Nogales

    (Lawrence Berkeley National Laboratory
    Howard Hughes Medical Institute, University of California)

Abstract

The Ndc80 complex is a key site of regulated kinetochore–microtubule attachment (a process required for cell division), but the molecular mechanism underlying its function remains unknown. Here we present a subnanometre-resolution cryo-electron microscopy reconstruction of the human Ndc80 complex bound to microtubules, sufficient for precise docking of crystal structures of the component proteins. We find that the Ndc80 complex binds the microtubule with a tubulin monomer repeat, recognizing α- and β-tubulin at both intra- and inter-tubulin dimer interfaces in a manner that is sensitive to tubulin conformation. Furthermore, Ndc80 complexes self-associate along protofilaments through interactions mediated by the amino-terminal tail of the NDC80 protein, which is the site of phospho-regulation by Aurora B kinase. The complex’s mode of interaction with the microtubule and its oligomerization suggest a mechanism by which Aurora B could regulate the stability of load-bearing kinetochore–microtubule attachments.

Suggested Citation

  • Gregory M. Alushin & Vincent H. Ramey & Sebastiano Pasqualato & David A. Ball & Nikolaus Grigorieff & Andrea Musacchio & Eva Nogales, 2010. "The Ndc80 kinetochore complex forms oligomeric arrays along microtubules," Nature, Nature, vol. 467(7317), pages 805-810, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7317:d:10.1038_nature09423
    DOI: 10.1038/nature09423
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    Cited by:

    1. Erik Zupa & Martin Würtz & Annett Neuner & Thomas Hoffmann & Mandy Rettel & Anna Böhler & Bram J. A. Vermeulen & Sebastian Eustermann & Elmar Schiebel & Stefan Pfeffer, 2022. "The augmin complex architecture reveals structural insights into microtubule branching," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Yusuke Takenoshita & Masatoshi Hara & Tatsuo Fukagawa, 2022. "Recruitment of two Ndc80 complexes via the CENP-T pathway is sufficient for kinetochore functions," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    3. Sophie M. Travis & Brian P. Mahon & Wei Huang & Meisheng Ma & Michael J. Rale & Jodi Kraus & Derek J. Taylor & Rui Zhang & Sabine Petry, 2023. "Integrated model of the vertebrate augmin complex," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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