title: Processive kinesins require loose mechanical coupling for efficient collective motility.
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.
authors.affiliation: Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
authors.forename: Peter
authors.initials: P
authors.lastname: Bieling
authors.forename: Ivo A
authors.initials: IA
authors.lastname: Telley
authors.forename: Jacob
authors.initials: J
authors.lastname: Piehler
authors.forename: Thomas
authors.initials: T
authors.lastname: Surrey
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D020409:Molecular Motor Proteins / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D020409:Molecular Motor Proteins; D016547:Kinesins