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Embedding dual function into molecular motors through collective motion.

Nen Saito1, Kunihiko Kaneko1,2

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The directionality of kinesin-5 Cin8 motors changes based on the number of motors on a microtubule. This collective behavior, like a tug-of-war, allows motors to switch directions, impacting cellular processes.

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Area of Science:

  • Molecular motor function
  • Cellular mechanics
  • Biophysics

Background:

  • Protein motors like kinesins and dyneins move directionally along microtubules.
  • Previously, motor directionality was assumed constant without external forces.
  • Kinesin-5 Cin8 motor directionality was recently observed to change with increased motor numbers.

Purpose of the Study:

  • To introduce a mechanical model for microtubule-sliding assays with multiple interacting motors.
  • To investigate how collective motor behavior influences motor directionality.
  • To explore the implications of context-dependent motor function in cellular processes.

Main Methods:

  • Developed a simple mechanical model of a microtubule-sliding assay.
  • Simulated interactions between multiple protein motors and a microtubule filament.
  • Analyzed the influence of motor number on motor directionality and movement.

Main Results:

  • Motor directionality can change (e.g., minus- to plus- end) based on the number of motors.
  • This switch is driven by a large diffusive component and frustrated motor configurations (tug-of-war).
  • Collective phenomena dictate motor behavior in multi-motor systems.

Conclusions:

  • Motor directionality is not always constant and can be context-dependent.
  • A collective, tug-of-war mechanism explains the observed changes in motor directionality.
  • This framework offers insights into dual-directional motors and their role in mitotic spindle formation.