Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 23, Issue 24, Pages 4786-4795Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E12-03-0214
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Funding
- Searle Scholars Program
- Human Frontiers Science Foundation
- National Institutes of Health/National Institute of General Medical Sciences [GM088313]
- Cancer Research UK
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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.
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