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KIF14 Binds Tightly to Microtubules and Adopts a Rigor-Like Conformation.

Arora K, Talje L, Asenjo AB, Andersen P, Atchia K, Joshi M, Sosa H, Allingham JS, Kwok BH

Department of Biomedical and Molecular Sciences, Queen's University, 18 Stuart St., Rm. 652, Kingston, ON K7L 3 N6, Canada.

The mitotic kinesin motor protein KIF14 is essential for cytokinesis during cell division and has been implicated in cerebral development and a variety of human cancers. Here we show that the mouse KIF14 motor domain binds tightly to microtubules and does not display typical nucleotide-dependent changes in this affinity. It also has robust ATPase activity but very slow motility. A crystal structure of the ADP-bound form of the KIF14 motor domain reveals a dramatically opened ATP-binding pocket, as if ready to exchange its bound ADP for Mg·ATP. In this state, the central β-sheet is twisted ~10° beyond the maximal amount observed in other kinesins. This configuration has only been seen in the nucleotide-free states of myosins-known as the "rigor-like" state. Fitting of this atomic model to electron density maps from cryo-electron microscopy indicates a distinct binding configuration of the motor domain to microtubules. We postulate that these properties of KIF14 are well suited for stabilizing midbody microtubules during cytokinesis.

J. Mol. Biol. 2014;426(17):2997-3015.

Pubmed ID: 24949858

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