%0 Journal Article
%T Multiple phosphorylations control recruitment of the KMN network onto kinetochores
%J -
%D 2018
%R https://doi.org/10.1038/s41556-018-0230-0
%X To establish a functional kinetochore, the constitutive centromere-associated network (CCAN) forms a foundation on the centromere and recruits the KMN network, which directly binds to spindle microtubules. The CENP-C and CENP-T pathways in the CCAN recruit the KMN network to kinetochores, independently. The CENP-C pathway has been considered the major scaffold for the KMN network in vertebrate CCAN. However, we demonstrate that it is mainly the CENP-T pathway that recruits the KMN network onto the kinetochores and that CENP-T¨CKMN interactions are essential in chicken DT40 cells. By contrast, less Ndc80 binds to the CENP-C pathway in mitosis and the Mis12¨CCENP-C association is decreased during mitotic progression, which is consistent with the finding that the Mis12 complex¨CCENP-C binding is dispensable for cell viability. Furthermore, we find that multiple phosphoregulations of CENP-T and the Mis12 complex make the CENP-T pathway dominant. These results provide key insights into kinetochore dynamics during mitotic progression
%U https://www.nature.com/articles/s41556-018-0230-0