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Issue 24, 2009
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Negative interference dominates collective transport of kinesin motors in the absence of load

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Abstract

The collective function of motor proteins is known to be important for the directed transport of many intracellular cargos. However, understanding how multiple motors function as a group remains challenging and requires new methods that enable determination of both the exact number of motors participating in motility and their organization on subcellular cargos. Here we present a biosynthetic method that enables exactly two kinesin-1 molecules to be organized on linear scaffolds that separate the motors by a distance of 50 nm. Tracking the motions of these complexes revealed that while two motors produce longer average run lengths than single kinesins, the system effectively behaves as though a single-motor attachment state dominates motility. It is proposed that negative motor interference derived from asynchronous motor stepping and the communication of forces between motors leads to this behavior by promoting the rapid exchange between different microtubule-bound configurations of the assemblies.

Graphical abstract: Negative interference dominates collective transport of kinesin motors in the absence of load

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Article information


Submitted
16 Jan 2009
Accepted
16 Mar 2009
First published
20 Apr 2009

Phys. Chem. Chem. Phys., 2009,11, 4882-4889
Article type
Paper

Negative interference dominates collective transport of kinesin motors in the absence of load

A. R. Rogers, J. W. Driver, P. E. Constantinou, D. Kenneth Jamison and M. R. Diehl, Phys. Chem. Chem. Phys., 2009, 11, 4882
DOI: 10.1039/B900964G

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