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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...

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...

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 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...

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.

Actin Polymerization and Cell Motility

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.

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Related Experiment Video

Updated: May 17, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Spontaneous structural changes in actin regulate G-F transformation.

Masatoshi Morimatsu¹, Yuichi Togashi, So Nishikawa

¹Nanobiology Laboratories, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.

|November 13, 2012

Summary

This summary is machine-generated.

Actin monomers (G-actin) transition to polymers (F-actin) through conformational changes. These structural shifts, occurring over hundreds of seconds, are environment-dependent, facilitating actin polymerization crucial for cell functions.

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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Related Experiment Videos

Last Updated: May 17, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Area of Science:

Biochemistry and Molecular Biology
Cellular Dynamics
Biophysics

Background:

Actin's monomeric (G-actin) and polymeric (F-actin) forms are crucial for cellular processes like migration and division.
Understanding the conformational transitions between G-actin and F-actin is key to elucidating these dynamic cellular behaviors.

Purpose of the Study:

To investigate the conformational changes of individual actin protomers during transitions between G-actin and F-actin.
To determine the timescale and environmental influences on these actin structural dynamics.

Main Methods:

Utilized single-molecule Förster resonance energy transfer (smFRET) microscopy.
Employed total internal reflection fluorescence (TIRF) microscopy to observe individual actin protomers.

Main Results:

Identified distinct conformational states for individual actin protomers.
Observed that the transition between conformational states occurs over hundreds of seconds.
Demonstrated that the distribution of these states is influenced by the surrounding cellular environment.

Conclusions:

Actin protomers exhibit dynamic conformational flexibility.
Environmental factors play a significant role in modulating actin's structural states.
These spontaneous structural changes enable actin to adapt for polymerization, supporting cellular functions.