Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Actin Polymerization01:42

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 Motility01:13

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.
Generation of Straight or Branched Actin Filaments01:14

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...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Introduction to Actin01:26

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 Filaments01:11

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...

You might also read

Related Articles

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

Sort by
Same author

Nuclear mechanobiology in confined cell migration.

Nucleus (Austin, Tex.)·2026
Same author

Evidence for Drop-Like Nuclear Deformation in Sheared Endothelial Monolayers.

Small (Weinheim an der Bergstrasse, Germany)·2025
Same author

Micropost Arrays to Model ECM Fiber Obstacles During Cell Migration in Confinement.

Methods in molecular biology (Clifton, N.J.)·2025
Same author

Excess surface area of the nuclear lamina enables unhindered cell migration through constrictions.

Science advances·2025
Same author

Matrix stiffness drives drop like nuclear deformation and lamin A/C tension-dependent YAP nuclear localization.

Nature communications·2024
Same author

Rethinking nuclear shaping: insights from the nuclear drop model.

Soft matter·2024
Same journal

A perception-memory PDE framework for seasonal migration dynamics.

Journal of mathematical biology·2026
Same journal

Dynamic resource allocation in eukaryotic Resource Balance Analysis.

Journal of mathematical biology·2026
Same journal

Discrete-time exploitative competition model of different stage-specific predators.

Journal of mathematical biology·2026
Same journal

Spatiotemporal SEIQR Epidemic Modeling with Optimal Control for Vaccination, Treatment, and Social Measures.

Journal of mathematical biology·2026
Same journal

Phenotypic plasticity trade-offs in an age-structured model of bacterial growth under stress.

Journal of mathematical biology·2026
Same journal

Intraspecific interactions facilitate mutualism across multilayer networks under weak selection.

Journal of mathematical biology·2026
See all related articles

Related Experiment Video

Updated: Jul 3, 2026

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
09:10

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

Published on: August 25, 2022

Models for actin polymerization motors.

Richard B Dickinson1

  • 1Departments of Chemical Engineering and Biomedical Engineering, University of Florida, Gainesville, FL, 32611, USA. dickinso@che.ufl.edu

Journal of Mathematical Biology
|July 10, 2008
PubMed
Summary
This summary is machine-generated.

This review compares two models of actin polymerization driving cell motility. It evaluates their predictions against experimental data, focusing on filament-end dynamics and the role of end-tracking proteins.

More Related Videos

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

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

Related Experiment Videos

Last Updated: Jul 3, 2026

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
09:10

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

Published on: August 25, 2022

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

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

Area of Science:

  • Cell biology
  • Biophysics
  • Biochemistry

Background:

  • Actin polymerization powers cell movement and pathogen propulsion.
  • The precise molecular mechanisms of actin-based motility remain incompletely understood.
  • Existing models explain force generation but not all observed phenomena.

Purpose of the Study:

  • To compare two major classes of actin polymerization models.
  • To evaluate model predictions against experimental data.
  • To assess the role of end-tracking proteins in actin-based motility.

Main Methods:

  • Comparative analysis of theoretical models.
  • Evaluation of force-velocity profiles.
  • Review of experimental evidence from biomimetic particles and protein studies.

Main Results:

  • Two distinct models exist: free filament-end addition versus persistent surface association.
  • Model predictions differ regarding force-velocity relationships.
  • End-tracking proteins like formins are crucial for actin-based motility.

Conclusions:

  • The "actoclampin" model better explains persistent network attachment.
  • Experimental data support models involving filament end-tracking proteins.
  • Further research is needed to fully elucidate actin polymerization dynamics in motility.