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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...

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.

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

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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

Biphasic interactions between a cationic dendrimer and actin.

Pakatip Ruenraroengsak¹, Alexander T Florence

¹Centre for Drug Delivery Research (CDDR), The School of Pharmacy, University of London, London, UK.

Journal of Drug Targeting

|October 12, 2010

Summary

Cationic dendrimers interact with actin filaments, influencing their polymerization. This interaction affects dendrimer transport and suggests potential anticancer applications by modulating actin dynamics.

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Synthesis, Cellular Delivery and In vivo Application of Dendrimer-based pH Sensors

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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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Synthesis, Cellular Delivery and In vivo Application of Dendrimer-based pH Sensors

Synthesis, Cellular Delivery and In vivo Application of Dendrimer-based pH Sensors

Published on: September 10, 2013

Area of Science:

Biomaterials Science
Cell Biology
Nanotechnology

Background:

Gene delivery systems face challenges navigating crowded cellular environments, including the cytoplasm and nucleus.
Actin networks in the cytoplasm present a significant physical barrier to nanoparticle diffusion.
Understanding nanoparticle-cytoskeletal interactions is crucial for effective intracellular delivery.

Purpose of the Study:

To investigate the interaction between a cationic dendrimer and actin filaments in vitro.
To determine how this interaction affects dendrimer diffusion and actin polymerization dynamics.
To explore the potential implications for gene delivery and therapeutic applications, such as anticancer treatments.

Main Methods:

Utilized a self-fluorescent sixth-generation cationic dendrimer (6 nm diameter).
Performed in vitro studies to assess dendrimer-actin filament interactions.
Analyzed the effects of varying dendrimer concentrations on actin polymerization kinetics.

Main Results:

The cationic dendrimer exhibits reversible, potentially electrostatic, interactions with actin filaments.
These interactions lead to biphasic effects on actin polymerization: inhibition at low concentrations and acceleration at high concentrations.
Dendrimer diffusion is modulated by its interaction with the actin network.

Conclusions:

Cationic dendrimer transport within cells is influenced by both physical and chemical interactions with the actin cytoskeleton.
The biphasic modulation of actin polymerization suggests a complex role in cellular transport.
The dendrimer's inhibitory effect on actin polymerization indicates potential as an anticancer agent.