The mitotic kinesin-14 KlpA contains a context-dependent directionality switch

Andrew R. Popchock, Kuo-Fu Tseng, Pan Wang, P. Andrew Karplus, Xin Xiang and Weihong Qiu ()
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Andrew R. Popchock: Oregon State University
Kuo-Fu Tseng: Oregon State University
Pan Wang: Oregon State University
P. Andrew Karplus: Oregon State University
Xin Xiang: The Uniformed Services University of the Health Sciences
Weihong Qiu: Oregon State University

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract Kinesin-14s are commonly known as nonprocessive minus end-directed microtubule motors that function mainly for mitotic spindle assembly. Here we show using total internal reflection fluorescence microscopy that KlpA—a kinesin-14 from Aspergillus nidulans—is a context-dependent bidirectional motor. KlpA exhibits plus end-directed processive motility on single microtubules, but reverts to canonical minus end-directed motility when anchored on the surface in microtubule-gliding experiments or interacting with a pair of microtubules in microtubule-sliding experiments. Plus end-directed processive motility of KlpA on single microtubules depends on its N-terminal nonmotor microtubule-binding tail, as KlpA without the tail is nonprocessive and minus end-directed. We suggest that the tail is a de facto directionality switch for KlpA motility: when the tail binds to the same microtubule as the motor domain, KlpA is a plus end-directed processive motor; in contrast, when the tail detaches from the microtubule to which the motor domain binds, KlpA becomes minus end-directed.

Date: 2017
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DOI: 10.1038/ncomms13999

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