The microtubule-binding protein Cep170 promotes the targeting of the kinesin-13 depolymerase Kif2b to the mitotic spindle

J.P.I. Welburn, I.M. Cheeseman

Research output: Contribution to journalArticlepeer-review

Abstract

Microtubule dynamics are essential throughout mitosis to ensure correct chro mosome segregation. Microtubule depolymerization is controlled in part by microtubule de polymerases, 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. How ever, 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.
Original languageEnglish
Pages (from-to)4786-4795
Number of pages10
JournalMolecular Biology of the Cell
Volume23
Issue number24
DOIs
Publication statusPublished - 15 Dec 2012

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