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Diffusion Biased by a Soft Neck Linker Regulates Kinesin Stepping.

Huijuan Xu1,2, Ruizheng Hou3, Tong Tong1,2

  • 1School of Physics, Xi'an Jiaotong University, Xi'an 710049, China.

The Journal of Physical Chemistry. B
|March 5, 2021
PubMed
Summary

Kinesin motors move along microtubules, but the mechanism for their directional stepping was unclear. A new kinetic model explains this directionality through neck linker zippering and ATP catalysis, validated by experimental data.

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Area of Science:

  • Molecular motor function
  • Biophysics
  • Cellular transport

Background:

  • Conventional kinesin is a microtubule-associated motor protein essential for intracellular transport.
  • Kinesin's primary movement is towards the microtubule plus end, but occasional backward steps occur.
  • The precise physical mechanism governing kinesin's directional stepping remains incompletely understood.

Purpose of the Study:

  • To develop and validate a kinetic model explaining kinesin's forward and backward stepping mechanism.
  • To elucidate the role of neck linker zippering and ATP catalysis in kinesin directionality.
  • To identify the physical mechanism regulating kinesin stepping via biased diffusion.

Main Methods:

  • Development of a two-cycle kinetic model incorporating kinesin forward and backward stepping.
  • Quantitative validation of the model using experimental data (load dependence, stepping ratio, dwell time).
  • Analysis of load dependence and thermodynamic properties to identify the stepping mechanism.

Main Results:

  • The kinetic model accurately predicts experimental observations of kinesin stepping behavior.
  • A biased diffusion process was identified as the mechanism regulating kinesin stepping.
  • Model suggests kinesin directionality is optimized under a thermodynamic constraint.

Conclusions:

  • The study provides a chemomechanical coupling mechanism for kinesin directionality.
  • Neck linker flexibility and zippering are crucial for rectifying kinesin's direction.
  • The model integrates kinesin's performance and directionality into a consistent framework.