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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.

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.

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...

Synteny and Evolution

Synteny and Evolution

John H. Renwick first coined the term “synteny” in 1971, which refers to the genes present on the same chromosomes, even if they are not genetically linked. The species with common ancestry tend to show conserved syntenic regions. Therefore, the concept of synteny is nowadays used to describe the evolutionary relationship between species.
Around 80 million years ago, the human and mice lineages diverged from the common ancestor. During the course of evolution, the ancestral chromosome underwent...

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Related Experiment Video

Updated: May 9, 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

Dynamic actin gene family evolution in primates.

Liucun Zhu¹, Ying Zhang, Yijun Hu

¹Institute of System Biology, Shanghai University, Shanghai 200444, China.

Biomed Research International

|July 11, 2013

Summary

Primates possess numerous actin genes, with evolutionary patterns suggesting a "birth and death" model. This process involves gene duplication and loss, leading to increased functional complexity and adaptation.

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Last Updated: May 9, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Published on: July 30, 2014

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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

Area of Science:

Genomics
Evolutionary Biology
Molecular Biology

Background:

Actin proteins are highly conserved and essential for eukaryotic cellular functions.
Actin is encoded by multigene families, yet comparative studies across primate species are limited.

Purpose of the Study:

To systematically investigate the characteristics and evolutionary patterns of the actin gene family in primates.
To compare actin gene family evolution across seven primate species.

Main Methods:

Genome-wide identification of actin genes in human, chimpanzee, gorilla, orangutan, gibbon, rhesus monkey, and marmoset.
Phylogenetic analysis to determine evolutionary relationships.
Analysis of codon usage, gene expression, and pseudogene identification.

Main Results:

Identified 233 actin genes across the seven primate genomes.
Phylogenetic analysis revealed two major clades: orthologous and complex groups.
Actin gene copies showed conserved codon usage and expression but diverged within species; numerous pseudogenes were detected.

Conclusions:

The primate actin gene family likely evolved via a
birth and death
model.
This evolutionary process involves gene duplication, loss, and negative selection, enhancing functional complexity.