The Ndc80 kinetochore complex forms oligomeric arrays along microtubules.

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.

journal_name

Nature

journal_title

Nature

authors

Alushin GM,Ramey VH,Pasqualato S,Ball DA,Grigorieff N,Musacchio A,Nogales E

doi

10.1038/nature09423

subject

Has Abstract

pub_date

2010-10-14 00:00:00

pages

805-10

issue

7317

eissn

0028-0836

issn

1476-4687

pii

nature09423

journal_volume

467

pub_type

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