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Related Concept Videos

Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Related Experiment Video

Updated: May 25, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
06:53

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Rotational model for actin filament alignment by myosin.

Callie J Miller1, G Bard Ermentrout, Lance A Davidson

  • 1Department of Bioengineering, University of Pittsburgh, Pittsburgh, PA, USA.

Journal of Theoretical Biology
|February 14, 2012
PubMed
Summary

This study reveals how myosin motors align actin filaments, crucial for cell shape and movement. Optimal motor speed is key, but filament growth and shrinkage disrupt this alignment, creating stable cellular structures.

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Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Last Updated: May 25, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

Published on: February 4, 2021

Area of Science:

  • Cell Biology
  • Biophysics
  • Cytoskeletal Dynamics

Background:

  • Actomyosin cytoskeleton dynamics are essential for cellular functions like motility and division.
  • Previous models focused on actin filament translation, neglecting filament rotation's role in cell mechanics.

Purpose of the Study:

  • To explicitly model actin filament rotation dynamics driven by myosin II motors.
  • To investigate how filament rotation influences cell shape, movement, and force generation.

Main Methods:

  • Utilized Monte Carlo simulations to model myosin II motor interactions with actin filament pairs.
  • Employed continuum models to analyze the stability and force-generating capabilities of filament arrays.
  • Incorporated actin filament polymerization/depolymerization and myosin motor stretch into the models.

Main Results:

  • Identified an optimal myosin motor velocity for efficient actin filament alignment.
  • Demonstrated that polymerization and depolymerization lead to reduced alignment and stable, asynchronous filament arrays.
  • Found that two distinct F-actin array morphologies can generate equivalent forces.
  • Discovered a phase transition to alignment under conditions of reduced polymerization or optimized motor velocity.

Conclusions:

  • Actin filament rotation by myosin II motors is a critical factor in cytoskeletal organization and force generation.
  • The interplay between motor dynamics, filament turnover, and structural morphology dictates cellular mechanical properties.
  • This integrated simulation and continuum analysis approach provides novel insights into cytoskeletal regulation.