title: Elastic Anisotropy Scenario for Cooperative Binding of Kinesin-Coated Beads on Microtubules.
abstract: Muto et al. reported in 2005 an observation called cooperative binding, according to which the initial binding of a bead covered with active kinesins on a microtubule filament was capable of favoring the subsequent binding of similar beads on the same filament up to distances of the order of a few microns. This positive bias is stronger ahead of the initially bound bead than behind. We explain this effect by combining the recently proposed notion of shear screening length with the notion of localized tubulin conformational transition induced by motor binding. Elastic terms linked to the polarity of protofilaments, up to now ignored, provide adequate description to the long-range elastic shear generated by motor binding. The subsequent binding is favored when and where the shear displacement of protofilaments meets the requirement for specific strong binding. We propose experimental tests of our model, which open the way to a new type of spectroscopy for biomolecular processes.
authors.affiliation: Matières et Systèmes Complexes, CNRS-UMR7057, Université Paris-Diderot , 75205 Paris, France.|Gulliver, CNRS-UMR7083, ESPCI, 75231 Paris, France.
authors.forename: Ken
authors.initials: K
authors.lastname: Sekimoto
authors.affiliation: Physico-chimie Curie, CNRS-UMR168, Institut Curie , 75231 Paris, France.|Mechanobiology Institute, National University of Singapore , 5A Engineering Drive 1, 117411 Singapore.
authors.forename: Jacques
authors.initials: J
authors.lastname: Prost
mesh_terms: D016880:Anisotropy; D001696:Biomechanical Phenomena; D004548:Elasticity; D016547:Kinesins / Q000737:chemistry*; D008870:Microtubules / Q000737:chemistry* / Q000648:ultrastructure; D011485:Protein Binding; D033081:Shear Strength; D013816:Thermodynamics; D014404:Tubulin / Q000737:chemistry*
chemical_list: D014404:Tubulin; D016547:Kinesins