Biophysical Journal · 2012 · 67 citations · 15 references
Life SciencesCell BiologyMolecular BiologyCytoskeletonMolecular BiophysicsMotor ControlCytoskeletal DynamicsCytoskeletal MechanicsCytoskeleton DynamicsMicrotubule-associated ProteinsMolecular MotorsMotor ProteinsDirectional MotilityKinesin MotilityKinesin MotorsKinesin-mediated MotilityMicrotubule MechanicsMotility MechanismsMotor Protein DynamicsMotor Protein Processivity
Kinesin-1 motor proteins walk parallel to the protofilament axes of microtubules as they step from one tubulin dimer to the next. Is protofilament tracking an inherent property of processive kinesin motors, like kinesin-1, and what are the structural determinants underlying protofilament tracking? To address these questions, we investigated the tracking properties of the processive kinesin-8, Kip3. Using in vitro gliding motility assays, we found that Kip3 rotates microtubules counterclockwise around their longitudinal axes with periodicities of ∼1 μm. These rotations indicate that the motors switch protofilaments with a bias toward the left. Molecular modeling suggests 1), that the protofilament switching may be due to kinesin-8 having a longer neck linker than kinesin-1, and 2), that the leftward bias is due the asymmetric geometry of the motor neck linker complex.
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A structural change in the kinesin motor protein that drives motility
Sarah E. Rice, Abel W. Lin, Daniel Safer et al. · Nature · 1999 · 811 citations
Yeast kinesin-8 depolymerizes microtubules in a length-dependent manner
Vladimír Varga, Jonne Helenius, Kozo Tanaka et al. · Nature Cell Biology · 2006 · 467 citations
The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility
Frank Kozielski, Stefan Sack, Alexander Marx et al. · Cell · 1997 · 411 citations · Full text
Kinesin follows the microtubule's protofilament axis.
Sanghamitra Ray, Edgar Meyhöfer, Ronald A. Milligan et al. · The Journal of Cell Biology · 1993 · 352 citations · Full text