A model of processive walking and slipping of kinesin-8 molecular motors

Ping Xie1

  • 1Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, 100190, China. pxie@aphy.iphy.ac.cn.

Scientific Reports
|April 14, 2021
PubMed

Insights

This study models the kinesin-8 motor

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Motor Dynamics

Background:

  • Kinesin-8 motors exhibit superprocessive movement along microtubules, fueled by ATP hydrolysis and microtubule depolymerization.
  • Single-molecule studies reveal frequent stick-slip motion interrupting the superprocessive movement of yeast kinesin-8 (Kip3).

Purpose of the Study:

  • To develop a chemomechanical model for kinesin-8 motor function.
  • To analytically investigate the dynamics of the Kip3 motor using the proposed model.

Main Methods:

  • Development of a novel chemomechanical model for kinesin-8.
  • Analytical investigation of motor dynamics under varying conditions (ATP, ADP, external load).

Main Results:

  • The model quantitatively reproduces existing single-molecule data for kinesin-8 velocity under different load conditions.
  • The model accurately predicts motor behavior with and without slip, and under varying nucleotide states (ATP, ADP).
  • Predictions are provided for load-dependent stepping ratios and velocities.

Conclusions:

  • The developed model provides a robust framework for understanding kinesin-8 chemomechanical coupling and dynamics.
  • The model's ability to replicate experimental data highlights its predictive power for kinesin motor function.
  • Insights into the similarities and differences between kinesin-8 and kinesin-1 dynamics are discussed.

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