Aurora B switches relative strength of kinetochore–microtubule attachment modes for error correction

Harinath Doodhi (Lead / Corresponding author), Taciana Kasciukovic, Lesley Clayton, Tomoyuki U. Tanaka (Lead / Corresponding author)

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    8 Citations (Scopus)
    153 Downloads (Pure)

    Abstract

    To establish chromosome bi-orientation, aberrant kinetochore–microtubule interaction must be resolved (error correction) by Aurora B kinase. Aurora B differentially regulates kinetochore attachment to the microtubule plus end and its lateral side (end-on and lateral attachment, respectively). However, it is still unclear how kinetochore–microtubule interactions are exchanged during error correction. Here we reconstituted the budding yeast kinetochore–microtubule interface in vitro by attaching the Ndc80 complexes to nanobeads. These Ndc80C–nanobeads recapitulated in vitro the lateral and end-on attachments of authentic kinetochores, on dynamic microtubules loaded with the Dam1 complex. This in vitro assay enabled the direct comparison of lateral and end-on attachment strength and showed that Dam1 phosphorylation by Aurora B makes the end-on attachment weaker than the lateral attachment. Similar reconstitutions with purified kinetochore particles were used for comparison. We suggest the Dam1 phosphorylation weakens interaction with the Ndc80 complex, disrupts the end-on attachment and promotes the exchange to a new lateral attachment, leading to error correction.
    Original languageEnglish
    Article numbere202011117
    Number of pages14
    JournalJournal of Cell Biology
    Volume220
    Issue number6
    Early online date14 Apr 2021
    DOIs
    Publication statusPublished - 7 Jun 2021

    Keywords

    • Biochemistry
    • Biphysics
    • Cell cycle and division

    ASJC Scopus subject areas

    • Cell Biology

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