The microtubule-binding protein Cep170 promotes the targeting of the kinesin-13 depolymerase Kif2b to the mitotic spindle
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Welburn-2012-The microtubule-bind.pdf
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Author(s)
Welburn, Julie P. I.
Cheeseman, Iain M
Date Issued
October 2012
Journal
Molecular Biology of the Cell
Publisher
American Society for Cell Biology
Citation
Welburn, J. P. I., and I. M. Cheeseman. “The Microtubule-binding Protein Cep170 Promotes the Targeting of the Kinesin-13 Depolymerase Kif2b to the Mitotic Spindle.” Molecular Biology of the Cell 23.24 (2012): 4786–4795. © 2012 by The American Society for Cell Biology
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Final published version
Abstract
Microtubule dynamics are essential throughout mitosis to ensure correct chromosome segregation. Microtubule depolymerization is controlled in part by microtubule depolymerases, including the kinesin-13 family of proteins. In humans, there are three closely related kinesin-13 isoforms (Kif2a, Kif2b, and Kif2c/MCAK), which are highly conserved in their primary sequences but display distinct localization and nonoverlapping functions. Here we demonstrate that the N-terminus is a primary determinant of kinesin-13 localization. However, we also find that differences in the C-terminus alter the properties of kinesin-13, in part by facilitating unique protein–protein interactions. We identify the spindle-localized proteins Cep170 and Cep170R (KIAA0284) as specifically associating with Kif2b. Cep170 binds to microtubules in vitro and provides Kif2b with a second microtubule-binding site to target it to the spindle. Thus the intrinsic properties of kinesin-13s and extrinsic factors such as their associated proteins result in the diversity and specificity within the kinesin-13 depolymerase family.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1091/mbc.E12-03-0214
