IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v5y2014i1d10.1038_ncomms3964.html
   My bibliography  Save this article

Structural basis for microtubule recognition by the human kinetochore Ska complex

Author

Listed:
  • Maria Alba Abad

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh)

  • Bethan Medina

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh)

  • Anna Santamaria

    (Biozentrum, University of Basel)

  • Juan Zou

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh)

  • Carla Plasberg-Hill

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh)

  • Arumugam Madhumalar

    (National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India)

  • Uma Jayachandran

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh)

  • Patrick Marc Redli

    (Biozentrum, University of Basel)

  • Juri Rappsilber

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh
    Technische Universität Berlin)

  • Erich A. Nigg

    (Biozentrum, University of Basel)

  • A. Arockia Jeyaprakash

    (Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh)

Abstract

The ability of kinetochores (KTs) to maintain stable attachments to dynamic microtubule structures (‘straight’ during microtubule polymerization and ‘curved’ during microtubule depolymerization) is an essential requirement for accurate chromosome segregation. Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules.

Suggested Citation

  • Maria Alba Abad & Bethan Medina & Anna Santamaria & Juan Zou & Carla Plasberg-Hill & Arumugam Madhumalar & Uma Jayachandran & Patrick Marc Redli & Juri Rappsilber & Erich A. Nigg & A. Arockia Jeyaprak, 2014. "Structural basis for microtubule recognition by the human kinetochore Ska complex," Nature Communications, Nature, vol. 5(1), pages 1-14, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms3964
    DOI: 10.1038/ncomms3964
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms3964
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms3964?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms3964. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.