Journal
EMBO REPORTS
Volume 9, Issue 11, Pages 1121-1127Publisher
WILEY-BLACKWELL
DOI: 10.1038/embor.2008.169
Keywords
molecular motor; conventional kinesin; gliding assay; microtubule transport; surface immobilization
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Funding
- Deutsche Forschungsgemeinschaft
- German Federal Ministry of Education and Research (BMBF)
- European Commission (STREP 'Active Biomics')
- Swiss National Science Foundation
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Processive motor proteins are stochastic steppers that perform actual mechanical steps for only a minor fraction of the time they are bound to the filament track. Motors usually work in teams and therefore the question arises whether the stochasticity of stepping can cause mutual interference when motors are mechanically coupled. We used biocompatible surfaces to immobilize processive kinesin-1 motors at controlled surface densities in a mechanically well-defined way. This helped us to study quantitatively how mechanical coupling between motors affects the efficiency of collective microtubule transport. We found that kinesin-1 constructs that lack most of the non-motor sequence slow each other down when collectively transporting a microtubule, depending on the number of interacting motors. This negative interference observed for a motor ensemble can be explained quantitatively by a mathematical model using the known physical properties of individual molecules of kinesin-1. The non-motor extension of kinesin-1 reduces this mutual interference, indicating that loose mechanical coupling between motors is required for efficient transport by ensembles of processive motors.
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