title: Measurement of Force-Dependent Release Rates of Cytoskeletal Motors.
abstract: Optical tweezers permit measuring motor-filament rupture forces with piconewton sensitivity. For deeper structural and mechanistic understanding of motors, different structural constraints can be induced by pulling motor proteins at various positions and manipulating the direction of the exerted force. Here, we present an optical-trapping approach to investigate the effect of the magnitude and direction of tension applied to the linker element of cytoskeletal motors on motor-filament interactions. Using this approach, force-dependent microtubule release rates of monomeric kinesins can be directly measured by pulling on kinesin's "neck linker" with a constant force.
authors.affiliation: Department of Physics, University of California, Berkeley, CA, 94720, USA.
authors.forename: Sinan
authors.initials: S
authors.lastname: Can
authors.affiliation: Department of Physics and Department of Molecular and Cell Biology, University of California, Berkeley, CA, 94720, USA. yildiz@berkeley.edu.
authors.forename: Ahmet
authors.initials: A
authors.lastname: Yildiz
mesh_terms: D003599:Cytoskeleton / Q000737:chemistry* / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism; D008856:Microscopy, Fluorescence / Q000379:methods; D057054:Molecular Imaging / Q000379:methods; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism; D052898:Optical Tweezers; D055503:Protein Multimerization; D013194:Staining and Labeling
chemical_list: D020409:Molecular Motor Proteins; D004247:DNA; D016547:Kinesins
keywords: DNA tether; Gating; Interhead coordination; Kinesin; Molecular motors; Optical trapping; Rupture forces