Published online April 28, 2008
doi:10.1083/jcb.200802189
The Journal of Cell Biology, Vol. 181, No. 3, 411-419
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Kim et al.
CENP-E combines a slow, processive motor and a flexible coiled coil to produce an essential motile kinetochore tether
Yumi Kim1,2,
John E. Heuser5,
Clare M. Waterman6, and
Don W. Cleveland1,3,4
1 Ludwig Institute for Cancer Research, 2 Division of Biological Sciences, 3 School of Medicine, and 4 Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093
5 Department of Cell Biology, School of Medicine, Washington University, St. Louis, MO 63110
6 National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892
Correspondence to Don W. Cleveland: dcleveland{at}ucsd.edu
The mitotic kinesin centromere protein E (CENP-E) is an essential kinetochore component that directly contributes to the capture and stabilization of spindle microtubules by kinetochores. Although reduction in CENP-E leads to high rates of whole chromosome missegregation, neither its properties as a microtubule-dependent motor nor how it contributes to the dynamic linkage between kinetochores and microtubules is known. Using single-molecule assays, we demonstrate that CENP-E is a very slow, highly processive motor that maintains microtubule attachment for long periods. Direct visualization of full-length Xenopus laevis CENP-E reveals a highly flexible 230-nm coiled coil separating its kinetochore-binding and motor domains. We also show that full-length CENP-E is a slow plus end–directed motor whose activity is essential for metaphase chromosome alignment. We propose that the highly processive microtubule-dependent motor activity of CENP-E serves to power chromosome congression and provides a flexible, motile tether linking kinetochores to dynamic spindle microtubules.
Abbreviations used in this paper: CENP-E, centromere protein E; GMPCPP, guanosine-5'-([a,b]-methyleno) triphosphate; MSD, mean square displacement; TIRF, total internal reflection fluorescence.
© 2008 Kim et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
Related In this Issue article
-
CENP-E goes fishing for microtubules
- Mitch Leslie
J. Cell Biol. 2008 181: 399.
[Full Text]
[PDF]
This article has been cited by other articles:
-
Grissom, P. M., Fiedler, T., Grishchuk, E. L., Nicastro, D., West, R. R., Richard McIntosh, J.
(2009). Kinesin-8 from Fission Yeast: A Heterodimeric, Plus-End-directed Motor that Can Couple Microtubule Depolymerization to Cargo Movement. Mol. Biol. Cell
20: 963-972
[Abstract]
[Full Text]
-
Furuta, K., Edamatsu, M., Maeda, Y., Toyoshima, Y. Y.
(2008). Diffusion and Directed Movement: IN VITRO MOTILE PROPERTIES OF FISSION YEAST KINESIN-14 Pkl1. J. Biol. Chem.
283: 36465-36473
[Abstract]
[Full Text]
-
Buschmann, H., Lloyd, C. W.
(2008). Arabidopsis Mutants and the Network of Microtubule-Associated Functions. Mol Plant
1: 888-898
[Abstract]
[Full Text]
-
Leslie, M.
(2008). CENP-E goes fishing for microtubules. JCB
181: 399-399
[Full Text]
-
Tomishige, M.
(2008). Activation of mitotic kinesin by microtubule bundling. JCB
182: 417-419
[Abstract]
[Full Text]