Related Experiment Video
Updated: May 14, 2026

08:57
Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Acting on actin: the electric motility assay
D Riveline1, A Ott, F Jülicher
1Laboratoire PhysicoChimie Curie (associé au-Centre National de la Recherche Scientifique (CNRS), Institut Curie, Paris, France.
European Biophysics Journal : EBJ
|August 6, 1998
Summary
Researchers used electric fields to control actin filament motion on myosin, enabling exploration of force-velocity relationships and suggesting a dynamical phase transition.
Area of Science:
- Biophysics
- Cellular Mechanics
- Nanotechnology
Background:
- Actin filaments are crucial for cellular processes.
- Myosin motors drive actin motion.
- Controlling nanoscale motion is vital for bio-applications.
Purpose of the Study:
- To develop a novel technique for directing 2D actin filament motion.
- To investigate the force-velocity relationship of actin-myosin interactions under external fields.
- To explore potential dynamical phase transitions in actin-myosin systems.
Main Methods:
- Utilized a weak electric field parallel to the motion plane to direct actin filament movement.
- Employed poly(methylmethacrylate) (PMMA) gratings as rails for actin filaments.
- Analyzed filament velocity, force, effective friction, duty ratio, and stall force at varying myosin densities.
Main Results:
- Demonstrated control over actin filament velocity (increase, decrease, reversal) via electric field orientation and strength.
- Enabled exploration of three quadrants of the force-velocity diagram using PMMA gratings.
- Observed a discontinuity in the velocity-force relationship, indicative of a dynamical phase transition.
Conclusions:
- Electric field manipulation offers precise control over actin-myosin dynamics.
- The study provides new insights into the mechanical properties of actin-myosin interactions.
- A dynamical phase transition may occur in this system under specific conditions.
Related Concept Videos
Studying the Cytoskeleton
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
Actin Filament Depolymerization
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
Actin Polymerization and Cell Motility
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Actin Treadmilling
Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...

