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Published 9 October 2006. doi:10.1083/jcb.200606020
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 1, 41-53
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Article

Mapping the assembly pathways that specify formation of the trilaminar kinetochore plates in human cells



Song-Tao Liu1, Jerome B. Rattner2, Sandra A. Jablonski1, and Tim J. Yen1

1 Fox Chase Cancer Center, Philadelphia, PA 19111
2 Department of Cell Biology and Anatomy, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada

Correspondence to Tim J. Yen: TJ_Yen{at}fccc.edu

We report the interactions amongst 20 proteins that specify their assembly to the centromere–kinetochore complex in human cells. Centromere protein (CENP)-A is at the top of a hierarchy that directs three major pathways, which are specified by CENP-C, -I, and Aurora B. Each pathway consists of branches that intersect to form nodes that may coordinate the assembly process. Complementary EM studies found that the formation of kinetochore trilaminar plates depends on the CENP-I/NUF2 branch, whereas CENP-C and Aurora B affect the size, shape, and structural integrity of the plates. We found that hMis12 is not constitutively localized at kinetochores, and that it is not essential for recruiting CENP-I. Our studies also revealed that kinetochores in HeLa cells contain an excess of CENP-A, of which ~10% is sufficient to promote the assembly of normal levels of kinetochore proteins. We elaborate on a previous model that suggested kinetochores are assembled from repetitive modules (Zinkowski, R.P., J. Meyne, and B.R. Brinkley. 1991. J. Cell Biol. 113:1091–110).

Abbreviation used in this paper: ACA, anticentromere antibody.


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