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Related Experiment Videos

Motor-driven dynamics in actin-myosin networks.

Loïc Le Goff1, François Amblard, Eric M Furst

  • 1Institut Curie, Physico-Chimie Curie, UMR CNRS/IC 168, 26 rue d'Ulm, 75248 Paris Cedex 05, France.

Physical Review Letters
|January 22, 2002
PubMed
Summary

Myosin motor proteins enhance filamentous actin (F-actin) fluctuations, altering its rheological response. Depleting ATP causes a transient shift to a passive state, impacting F-actin dynamics.

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Area of Science:

  • Biophysics
  • Soft Matter Physics
  • Cellular Mechanics

Background:

  • Filamentous actin (F-actin) dynamics are crucial for cellular processes.
  • Motor proteins like myosin significantly influence F-actin's mechanical properties.
  • Understanding F-actin's rheology under active conditions is key to cell mechanics.

Purpose of the Study:

  • To investigate the impact of myosin motor protein activity on F-actin's rheological behavior.
  • To characterize the changes in F-actin viscoelasticity driven by motor proteins.
  • To explore the transition from active to passive F-actin states.

Main Methods:

  • Utilizing diffusing wave spectroscopy to probe F-actin dynamics.
  • Measuring the viscoelastic shear modulus G(d)(omega) under varying motor activity.
  • Employing single-filament measurements to determine apparent persistence length.

Main Results:

  • Saturating myosin activity enhances longitudinal F-actin fluctuations.
  • Viscoelastic shear modulus scales as G(d)(omega) approximately omega(7/8) with active motors.
  • ATP depletion induces a transient rigor state and shifts dissipation to transverse modes.

Conclusions:

  • Myosin motor activity increases the effective temperature for tangential F-actin motion.
  • The transition to a rigor state highlights the dynamic interplay between ATP and F-actin mechanics.
  • Motor-induced changes in F-actin rheology are significant for cellular functions.

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