Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization - PubMed (original) (raw)
. 2014 Feb 20;53(4):591-605.
doi: 10.1016/j.molcel.2014.01.019. Epub 2014 Feb 13.
Shyamal Mosalaganti 2, Jenny Keller 1, Marta Mattiuzzo 1, Katharina Overlack 1, Veronica Krenn 1, Anna De Antoni 3, Sabine Wohlgemuth 1, Valentina Cecatiello 4, Sebastiano Pasqualato 4, Stefan Raunser 2, Andrea Musacchio 5
Affiliations
- PMID: 24530301
- DOI: 10.1016/j.molcel.2014.01.019
Free article
Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization
Arsen Petrovic et al. Mol Cell. 2014.
Free article
Abstract
Faithful chromosome segregation is mandatory for cell and organismal viability. Kinetochores, large protein assemblies embedded in centromeric chromatin, establish a mechanical link between chromosomes and spindle microtubules. The KMN network, a conserved 10-subunit kinetochore complex, harbors the microtubule-binding interface. RWD domains in the KMN subunits Spc24 and Spc25 mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex, a KMN subcomplex that tethers directly onto the underlying chromatin layer. Here, we show that Knl1, a KMN subunit involved in mitotic checkpoint signaling, also contains RWD domains that bind the Mis12 complex and that mediate kinetochore targeting of Knl1. By reporting the first 3D electron microscopy structure of the KMN network, we provide a comprehensive framework to interpret how interactions of RWD-containing proteins with the Mis12 complex shape KMN network topology. Our observations unveil a regular pattern in the construction of the outer kinetochore.
Copyright © 2014 Elsevier Inc. All rights reserved.
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