Non-catalytic motor domains enable processive movement and functional diversification of the kinesin-14 Kar3

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Cite this article as: eLife 2015;4:e04489 doi: 10.7554/eLife.04489

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Abstract

Motors proteins of the conserved kinesin-14 family have important roles in mitotic spindle organization and chromosome segregation. Previous studies have indicated that kinesin-14 motors are non-processive enzymes, working in the context of multi-motor ensembles that collectively organize microtubule networks. Here we show that the yeast kinesin-14 Kar3 generates processive movement as a heterodimer with the non-motor proteins Cik1 or Vik1. By analyzing the single-molecule properties of engineered motors we demonstrate that the non-catalytic domain has a key role in the motility mechanism by acting as a 'foothold' that allows Kar3 to bias translocation towards the minus end. This mechanism rivals the speed and run length of conventional motors, can support transport of the Ndc80 complex in vitro and is critical for Kar3 function in vivo. Our findings provide an example for a non-conventional translocation mechanism and can explain how Kar3 substitutes for key functions of Dynein in the yeast nucleus.

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Christine Mieck

Research Institute of Molecular Pathology, Vienna, Austria

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The authors declare that no competing interests exist.
Maxim I Molodtsov

Research Institute of Molecular Pathology, Vienna, Austria

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The authors declare that no competing interests exist.
Katarzyna Drzewicka

Research Institute of Molecular Pathology, Vienna, Austria

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The authors declare that no competing interests exist.
Babet van der Vaart

Research Institute of Molecular Pathology, Vienna, Austria

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The authors declare that no competing interests exist.
Gabriele Litos

Research Institute of Molecular Pathology, Vienna, Austria

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The authors declare that no competing interests exist.
Gerald Schmauss

Research Institute of Molecular Pathology, Vienna, Austria

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The authors declare that no competing interests exist.
Alipasha Vaziri

Research Institute of Molecular Pathology, Vienna, Austria

Competing interests
The authors declare that no competing interests exist.
Stefan Westermann

Research Institute of Molecular Pathology, Vienna, Austria

For correspondence
westermann@imp.ac.at

Competing interests
The authors declare that no competing interests exist.

Reviewing Editor

Stephen C Harrison, Howard Hughes Medical Institute, Harvard Medical School, United States

Publication history

Received: August 23, 2014
Accepted: January 26, 2015
Accepted Manuscript published: January 27, 2015 (version 1)
Version of Record published: February 24, 2015 (version 2)

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This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.