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Related Experiment Video

Updated: Dec 4, 2025

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
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Backstepping Mechanism of Kinesin-1.

Algirdas Toleikis1, Nicholas J Carter1, Robert A Cross1

  • 1Centre for Mechanochemical Cell Biology, Warwick Medical School, Coventry, United Kingdom.

Biophysical Journal
|October 22, 2020
PubMed
Summary

All kinesin-1 backsteps are slips, not steps. This occurs after Pi release in the ATP cycle, allowing the motor to detach and reattach, maintaining movement under load.

Area of Science:

  • Cellular Biology
  • Biophysics
  • Molecular Motors

Background:

  • Kinesin-1 is a molecular motor that moves cellular cargo along microtubules.
  • Kinesin-1 typically moves forward but can move backward under load.
  • Large backward movements were previously thought to be slips, while smaller ones were considered steps.

Purpose of the Study:

  • To investigate the nature of kinesin-1 backward movements.
  • To determine if all kinesin-1 backsteps are slips.
  • To elucidate the mechanochemical cycle of kinesin-1 under load.

Main Methods:

  • Analyzing kinesin-1 stepping behavior under varying loads.
  • Comparing waiting times before forward steps, backsteps, and detachments.
  • Modifying microtubule type to alter backstep-to-detachment ratios.

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Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
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Main Results:

  • Kinesin-1 waits longer before backsteps and detachments than before forward steps.
  • Waiting times for backsteps and detachments are similar.
  • Changing microtubule type affects backstep/detachment ratios but not forward stepping.
  • Backsteps and detachments originate from a common state after Pi release.

Conclusions:

  • All kinesin-1 backsteps are slips, occurring after Pi release.
  • A proposed model suggests Pi release enables a weak-binding state allowing slips.
  • This 'rescued detachment' pathway is crucial for kinesin-1 processivity under load.