Work

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

Year: 2017

Type: article

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.

Source: Nature Communications

DOI: 10.1038/ncomms13999

Authors: Andrew R. Popchock, Kuo-Fu Tseng, Pan Wang, P. Andrew Karplus, Xin Xiang, Weihong Qiu

Institutions: Oregon State University, Henan University, Uniformed Services University of the Health Sciences

Language: English

Topic: Microtubule and mitosis dynamics

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $6,990

Funders: National Science Foundation, Oregon State University, University of California, Davis, University of California, San Francisco