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Actin Filament Depolymerization

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...

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...

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 Treadmilling

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...

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

Introduction to Actin

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.

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Related Experiment Video

Updated: Jun 29, 2026

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

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

Published on: July 11, 2025

Transient binding and dissipation in cross-linked actin networks.

O Lieleg¹, M M A E Claessens, Y Luan

¹Lehrstuhl für Biophysik E27, Technische Universität München, Germany.

Physical Review Letters

|October 15, 2008

Summary

Transiently cross-linked actin networks exhibit tunable viscoelasticity. Thermal unbinding of cross-links allows for stress relaxation and energy dissipation, crucial for biological functions.

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Last Updated: Jun 29, 2026

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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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

Area of Science:

Biophysics
Polymer Physics
Soft Matter Physics

Background:

Actin networks are crucial cytoskeletal components.
Transient cross-linking enables unique mechanical properties in biopolymer networks.
Understanding their viscoelasticity is key to cell mechanics.

Purpose of the Study:

To investigate the viscoelastic response of transiently cross-linked actin networks.
To elucidate the role of thermal cross-link unbinding in network dynamics.
To correlate microscopic events with macroscopic mechanical properties.

Main Methods:

Experimental characterization of actin network viscoelasticity.
Systematic variation of cross-linker off-rate, density, and solvent viscosity.
Development and application of a semiphenomenological model.

Main Results:

Transient cross-linking provides elasticity with local microstructure rearrangement.
Thermal unbinding induces stress relaxation and energy dissipation.
A model based on microscopic unbinding events accurately reproduces experimental frequency responses.

Conclusions:

Actin network viscoelasticity is governed by the dynamics of transient cross-links.
Tunable unbinding rates offer a mechanism for controlling network mechanical behavior.
The findings provide insights into the mechanics of cytoskeletal networks.