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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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Publication details

The article was received on 16 Jan 2009, accepted on 16 Mar 2009 and first published on 20 Apr 2009


Article type: Paper
DOI: 10.1039/B900964G
Citation: Phys. Chem. Chem. Phys., 2009,11, 4882-4889

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    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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