Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 426, Issue 17, Pages 2997-3015Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2014.05.030
Keywords
kinesin; KIF14; motor protein; microtubules; crystal structure
Categories
Funding
- Natural Sciences and Engineering Research Council of Canada
- Canadian Institutes of Health Research [MOP-97832, MOP-97928]
- Ontario Early Researcher Award program
- USA National Institutes of Health [R01-GM083338]
- Fonds de Recherche du Quebec-Sante Chercheure-Boursiere Junior 1 Award
- Canadian Institutes of Health Research New Investigator Award
- Institute for Research in Immunology and Cancer
- IRICoR - Canadian Center of Excellence in Commercialization and Research
- Canada Foundation for Innovation
- Fonds de Recherche du Quebec-Sante
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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 center dot ATP. In this state, the central beta-sheet is twisted similar to 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. (C) 2014 The Authors. Published by Elsevier Ltd.
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