Stable kinetochore-microtubule attachment is essential for cell division. It requires recruitment of outer kinetochore microtubule binders by centromere proteins C and T (CENP-C and CENP-T). To study the molecular requirements of kinetochore formation, we reconstituted the binding of the MIS12 and NDC80 outer kinetochore subcomplexes to CENP-C and CENP-T. Whereas CENP-C recruits a single MIS12:NDC80 complex, we show here that CENP-T binds one MIS12:NDC80 and two NDC80 complexes upon phosphorylation by the mitotic CDK1:Cyclin B complex at three distinct CENP-T sites. Visualization of reconstituted complexes by electron microscopy supports this model. Binding of CENP-C and CENP-T to MIS12 is competitive, and therefore CENP-C and CENP-T act in parallel to recruit two MIS12 and up to four NDC80 complexes. Our observations provide a molecular explanation for the stoichiometry of kinetochore components and its cell cycle regulation, and highlight how outer kinetochore modules bridge distances of well over 100 nm. © Huis in ’t Veld et al.

Priyanka Singh

Department of Bioscience & Bioengineering

IIT Jodhpur

P.J. Huisin’T Veld

S. Jeganathan

A. Petrovic

J. John

V. Krenn

F. Weissmann

T. Bange

A. Musacchio

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eLife

Molecular basis of outer kinetochore assembly on CENP-T

Journal	eLife
Publisher	eLife Sciences Publications Ltd
ISSN	2050084X