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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...

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.

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.

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...

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Related Experiment Video

Updated: Jun 6, 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

Dynamics of actin evolution in dinoflagellates.

Sunju Kim¹, Tsvetan R Bachvaroff, Sara M Handy

¹Smithsonian Environmental Research Center, Edgewater, Maryland, USA.

Molecular Biology and Evolution

|December 15, 2010

Summary

Dinoflagellate actin gene families show high similarity within and between closely related species, suggesting rapid evolution and potential pseudogenes. This pattern aligns with the "birth and death" model of gene family evolution.

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Last Updated: Jun 6, 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

Analyses of Actin Dynamics, Clutch Coupling and Traction Force for Growth Cone Advance

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Published on: October 21, 2021

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:

Molecular Evolution
Genomics
Marine Biology

Background:

Dinoflagellates possess unique genomes with high DNA content, complicating sequencing efforts.
Multicopy gene families are common in dinoflagellates, but their evolutionary dynamics remain poorly understood.
Comparative genomics across evolutionary scales is crucial for understanding gene family evolution.

Purpose of the Study:

To investigate the evolutionary dynamics of the actin gene family in closely related dinoflagellate species.
To compare sequence variation within and between Dinophysis acuminata and D. caudata.
To assess the suitability of actin for phylogenetic studies in closely related dinoflagellates.

Main Methods:

Sequencing of actin gene family members from Dinophysis acuminata and D. caudata.
Analysis of cDNA and genomic sequences to identify gene copies and pseudogenes.
Phylogenetic analysis of nucleotide sequences to infer evolutionary relationships and divergence.

Main Results:

Identified at least three types of actin sequences in the studied Dinophysis species.
Most actin copies were highly similar within species (8-10 nucleotide differences) and between species (12 nucleotide differences).
Discovered divergent sequences and potential pseudogenes (approx. 10%), consistent with the 'birth and death' model of gene evolution.

Conclusions:

Actin gene family evolution in these dinoflagellates is characterized by recent duplications, pseudogene formation, and incomplete lineage sorting.
The high degree of conservation and variation within species makes actin potentially unsuitable for fine-scale phylogenetic resolution in closely related dinoflagellates.
Findings contribute to understanding gene family dynamics in eukaryotes with complex genomes.