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Generation of Straight or Branched Actin Filaments

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...

Introduction to Actin

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across different species.

Overview of Myosin Structure and Function

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.

Formation of Higher-order Actin Filaments

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...

Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

Actin and Myosin in Muscle Contraction

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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...

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Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

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Published on: July 11, 2025

A coarse-grained molecular model for actin-myosin simulation.

William R Taylor¹, Zoe Katsimitsoulia

¹Division of Mathematical Biology, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. wtaylor@nimr.mrc.ac.uk

Journal of Molecular Graphics & Modelling

|August 21, 2010

Summary

We developed a coarse-grained molecular model to simulate myosin V movement on actin filaments. This model aids in understanding myosin

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Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

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Published on: August 25, 2022

Area of Science:

Biophysics
Molecular Dynamics
Computational Biology

Background:

Myosin V is crucial for intracellular transport along actin filaments.
Understanding myosin V's dynamic motion requires detailed molecular simulations.

Purpose of the Study:

To develop a coarse-grained molecular model for simulating myosin V on actin filaments.
To investigate myosin V binding interactions and conformational changes.

Main Methods:

Hierarchical molecular representation: secondary structures grouped into domains, then molecules.
Brownian-like translational and rotational motion for each level.
Steric exclusion and inter-domain restraints maintain molecular integrity.
Simulation of myosin dimer on actin filament, including loose and tight binding interactions.

Main Results:

Model stability tested in pre- and post-power-stroke conformations.
Simulations identified preferred myosin binding sites on the actin filament.
Effects of myosin twofold symmetry and cargo attachment were analyzed.

Conclusions:

The developed model provides a basis for dynamic simulations of myosin V processive motion.
This approach facilitates the study of molecular motors and their function.