Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

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.

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...

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...

Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

High-Bandwidth AFM Probes for Imaging in Air and Fluid.

Journal of microelectromechanical systems : a joint IEEE and ASME publication on microstructures, microactuators, microsensors, and microsystems·2026

Same author

Label-Free All-Electrical Tracking of Individual and Collective Cell Migration on a Megapixel CMOS Capacitance Sensor.

bioRxiv : the preprint server for biology·2026

Same author

Galvanin (TMEM154) is an electric-field sensor for directed cell migration.

Cell·2026

Same author

Partial EMT Drives Persistent Collective Migration via Collision Guidance in Heterogeneous Populations.

bioRxiv : the preprint server for biology·2026

Same author

Ultrasensitive measurement of brain penetration mechanics and blood vessel rupture with microscale probes.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Profiling extracellular matrix-driven heterogeneity of single cell migration and morphology.

Scientific reports·2026

Search research articles

Related Experiment Video

Updated: Jul 4, 2026

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

Electronically activated actin protein polymerization and alignment.

Ian Y Wong¹, Matthew J Footer, Nicholas A Melosh

¹Department of Materials Science & Engineering, Stanford University, Geballe Laboratory for Advanced Materials, 476 Lomita Mall, Stanford, California 94305, USA.

Journal of the American Chemical Society

|May 30, 2008

Summary

Researchers dynamically controlled protein polymerization using electronic fields. This method precisely regulates actin filament formation, creating novel biomimetic materials with applications in biopolymer self-assembly.

More Related Videos

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

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

Related Experiment Videos

Last Updated: Jul 4, 2026

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

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

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:

Biomaterials Science
Biophysics
Molecular Biology

Background:

Biological self-assembly relies on complex coordination of protein interactions, ion concentrations, and modifications.
Current biomimetic materials struggle to replicate the dynamic and diverse nature of biological self-assembly.

Purpose of the Study:

To demonstrate dynamic regulation of protein polymerization using electronically controlled ion mixing and monomer concentration.
To achieve unprecedented control over the formation of ordered macromolecular structures.

Main Methods:

Inhibited actin polymerization using low-ionic strength buffer.
Triggered nucleation and growth of actin filaments with low-frequency AC voltage, enhancing local monomer concentration and Mg(2+) mixing.
Independently controlled polymerization rate and filament orientation using combinations of low (100 Hz) and high (1 MHz) frequency AC voltages.

Main Results:

Achieved dynamic regulation of ion-sensitive protein polymerization.
Demonstrated voltage and frequency control over polymerization location, extent, rate, and filament orientation.
Created diverse macromolecular architectures, including hydrogel microparticles and aligned actin filament arrays with ~750 nm periodicity.

Conclusions:

Electronically enhanced ion mixing and monomer concentration offer a novel method for dynamic control of biopolymer self-assembly.
This approach is potentially applicable to a wide range of proteins and biopolymers activated by charged species.
Enables the creation of complex, ordered biomimetic structures with precise control over macromolecular architecture.