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 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 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.

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...

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...

You might also read

Related Articles

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

Sort by

Same author

Contractile forces direct the chiral swirling of minimal cell collectives.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

The molecular basis of lamin-specific chromatin interactions.

Nature structural & molecular biology·2025

Same author

Fabrication of microcompartments with controlled size and shape for encapsulating active matter.

Frontiers in cell and developmental biology·2025

Same author

AML patient blasts exhibit polarization defects upon interaction with bone marrow stromal cells.

EMBO reports·2025

Same author

Microtubule-driven cell shape changes and actomyosin flow synergize to position the centrosome.

The Journal of cell biology·2025

Same author

Filament transport supports contractile steady states of actin networks.

bioRxiv : the preprint server for biology·2025

Same journal

The Hedgehog Pathway Effector Smoothened Exhibits Signaling Competency in the Absence of Ciliary Accumulation.

Chemistry & biology·2017

Same journal

DIVERSE System: De Novo Creation of Peptide Tags for Non-enzymatic Covalent Labeling by In Vitro Evolution for Protein Imaging Inside Living Cells.

Chemistry & biology·2015

Same journal

Differential Regulation of Specific Sphingolipids in Colon Cancer Cells during Staurosporine-Induced Apoptosis.

Chemistry & biology·2015

Same journal

Synthetic Peptides as cGMP-Independent Activators of cGMP-Dependent Protein Kinase Iα.

Chemistry & biology·2015

Same journal

Unraveling the B. pseudomallei Heptokinase WcbL: From Structure to Drug Discovery.

Chemistry & biology·2015

Same journal

Vitamin C as Cancer Destroyer, Investigating Sulfhydration, and the Variability in CFTR Interactome.

Chemistry & biology·2015

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 18, 2026

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

Published on: August 25, 2022

Inhibitors target actin nucleators.

Laurent Blanchoin¹, Rajaa Boujemaa-Paterski

¹Institut de Recherches en Technologies et Sciences pour le Vivant, CNRS/CEA/INRA/UJF, Grenoble, France. laurent.blanchoin@cea.fr

Chemistry & Biology

|November 28, 2009

Summary

This summary is machine-generated.

Researchers identified a small molecule inhibitor for formin-mediated actin assembly. This discovery offers new tools for studying the relationship between actin nucleators and cellular structures.

More Related Videos

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

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

Related Experiment Videos

Last Updated: Jun 18, 2026

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

Published on: August 25, 2022

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

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Actin assembly is crucial for cellular structure and function.
Actin nucleators, such as formins and the Arp2/3 complex, regulate actin polymerization.
Understanding these processes is key to deciphering cellular dynamics.

Discussion:

Rizvi and colleagues report a novel small molecule inhibitor targeting formin-mediated actin assembly.
This inhibitor complements existing tools for studying actin dynamics.
The study provides a new chemical probe for cell biology research.

Key Insights:

Identification of a specific inhibitor for formin-mediated actin assembly.
Demonstration of the utility of small molecules in dissecting actin-related cellular processes.
Contribution to the toolkit for investigating the link between actin nucleators and cellular structures.

Outlook:

Further characterization of the inhibitor's mechanism of action.
Application of the inhibitor in diverse cell-based assays to explore actin dynamics.
Potential for developing new therapeutic strategies targeting actin-based cellular functions.