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Publication Abstract from PubMed

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 beta-sheet is twisted ~10 degrees 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.

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 J Mol Biol. 2014 Jun 17. pii: S0022-2836(14)00282-4. doi:, 10.1016/j.jmb.2014.05.030. PMID:24949858^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.