Processive kinesins require loose mechanical coupling for efficient collective motility
Open Access
- 19 September 2008
- journal article
- research article
- Published by Springer Nature in EMBO Reports
- Vol. 9 (11) , 1121-1127
- https://doi.org/10.1038/embor.2008.169
Abstract
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.Keywords
This publication has 28 references indexed in Scilit:
- How kinesin waits between stepsNature, 2007
- Detection of fractional steps in cargo movement by the collective operation of kinesin-1 motorsProceedings of the National Academy of Sciences, 2007
- The distance that kinesin-1 holds its cargo from the microtubule surface measured by fluorescence interference contrast microscopyProceedings of the National Academy of Sciences, 2006
- Single-Molecule Analysis of Dynein Processivity and Stepping BehaviorCell, 2006
- Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live CellsScience, 2002
- Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in waterNew Journal of Physics, 1999
- The Directional Preference of Kinesin Motors Is Specified by an Element outside of the Motor Catalytic DomainCell, 1997
- Failure of a single-headed kinesin to track parallel to microtubule protofilamentsNature, 1995
- Force and velocity measured for single kinesin moleculesCell, 1994
- Direct observation of kinesin stepping by optical trapping interferometryNature, 1993