CENP-F stabilizes kinetochore-microtubule attachments and limits dynein stripping of corona cargoes

CENP-F stabilizes kinetochore-microtubule attachments and limits dynein stripping of corona cargoes Accurate chromosome segregation demands efficient capture of microtubules by kinetochores and their conversion to stable bioriented attachments that can congress and then segregate chromosomes. An early event is the shedding of the outermost fibrous corona layer of the kinetochore following microtubule attachment. Centromere protein F (CENP-F) is part of the corona, contains two microtubule-binding domains, and physically associates with dynein motor regulators. Here, we have combined CRISPR gene editing and engineered separation-of-function mutants to define how CENP-F contributes to kinetochore function. We show that the two microtubule-binding domains make distinct contributions to attachment stability and force transduction but are dispensable for chromosome congression. We further identify a specialized domain that functions to limit the dynein-mediated stripping of corona cargoes through a direct interaction with Nde1. This antagonistic activity is crucial for maintaining the required corona composition and ensuring efficient kinetochore biorientation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Cell Biology Rockefeller University Press

CENP-F stabilizes kinetochore-microtubule attachments and limits dynein stripping of corona cargoes

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Publisher
Rockefeller University Press
Copyright
© 2020 Auckland et al.
ISSN
0021-9525
eISSN
1540-8140
DOI
10.1083/jcb.201905018
Publisher site
See Article on Publisher Site

Abstract

Accurate chromosome segregation demands efficient capture of microtubules by kinetochores and their conversion to stable bioriented attachments that can congress and then segregate chromosomes. An early event is the shedding of the outermost fibrous corona layer of the kinetochore following microtubule attachment. Centromere protein F (CENP-F) is part of the corona, contains two microtubule-binding domains, and physically associates with dynein motor regulators. Here, we have combined CRISPR gene editing and engineered separation-of-function mutants to define how CENP-F contributes to kinetochore function. We show that the two microtubule-binding domains make distinct contributions to attachment stability and force transduction but are dispensable for chromosome congression. We further identify a specialized domain that functions to limit the dynein-mediated stripping of corona cargoes through a direct interaction with Nde1. This antagonistic activity is crucial for maintaining the required corona composition and ensuring efficient kinetochore biorientation.

Journal

The Journal of Cell BiologyRockefeller University Press

Published: May 4, 2020

Keywords: kinetochores,microtubules,dynein atpase,rna, small interfering,centromere protein e,chromosome segregation,fluorescent antibody technique

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