Journal
MOLECULAR CELL
Volume 71, Issue 6, Pages 923-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2018.07.038
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Funding
- Max Planck Society
- European Research Council (ERC) Advanced Investigator Grant RECEPIANCE [669686]
- DFG's Collaborative Research Centre (CRC) [1093]
- Wellcome Trust Senior Investigator Award [106151/Z/14/Z]
- Royal Society Wolfson Research Merit Award [WM150020]
- European Research Council under the European Union's Seventh Framework Programme (FP7) [615984]
- Wellcome Trust [106151/Z/14/Z] Funding Source: Wellcome Trust
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The approximately thirty core subunits of kinetochores assemble on centromeric chromatin containing the histone H3 variant CENP-A and connect chromosomes with spindle microtubules. The chromatin proximal 16-subunit CCAN (constitutive centromere associated network) creates a mechanically stable bridge between CENP-A and the kinetochore's microtubule-binding machinery, the 10-subunit KMN assembly. Here, we reconstituted a stoichiometric 11-subunit human CCAN core that forms when the CENP-OPQUR complex binds to a joint interface on the CENP-HIKM and CENP-LN complexes. The resulting CCAN particle is globular and connects KMN and CENP-A in a 26-subunit recombinant particle. The disordered, basic N-terminal tail of CENP-Q binds microtubules and promotes accurate chromosome alignment, cooperating with KMN in microtubule binding. The N-terminal basic tail of the NDC80 complex, the microtubule-binding subunit of KMN, can functionally replace the CENP-Q tail. Our work dissects the connectivity and architecture of CCAN and reveals unexpected functional similarities between CENP-OPQUR and the NDC80 complex.
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