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Related Concept Videos

Actin Polymerization01:42

Actin Polymerization

8.0K
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...
8.0K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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...
3.6K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.4K
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...
3.4K
Introduction to Actin01:26

Introduction to Actin

6.1K
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...
6.1K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

6.2K
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....
6.2K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.6K
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...
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Related Experiment Video

Updated: Dec 14, 2025

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

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Insights into Actin Polymerization and Nucleation Using a Coarse-Grained Model.

Brandon G Horan1, Aaron R Hall1, Dimitrios Vavylonis1

  • 1Department of Physics, Lehigh University, Bethlehem, Pennsylvania.

Biophysical Journal
|July 16, 2020
PubMed
Summary

Molecular dynamics simulations reveal how actin monomers (G-actin) bind to growing filaments (F-actin). Monomers attach to both filament ends, influencing polymerization and nucleation pathways.

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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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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Area of Science:

  • Biophysics
  • Computational Biology
  • Cellular Dynamics

Background:

  • Actin polymerization is crucial for cell structure and motility.
  • Understanding actin nucleation and elongation kinetics is vital for cell biology.
  • Previous models relied on crystallographic and microscopy data.

Purpose of the Study:

  • To investigate actin filament polymerization and nucleation using molecular dynamics.
  • To identify equilibrium structural ensembles of interprotein complexes in actin.
  • To explore the binding dynamics of actin monomers at filament ends.

Main Methods:

  • Employed molecular dynamics simulations with a coarse-grained actin model.
  • Represented each actin residue as a single Cα interaction site.
  • Treated actin proteins as fully or partially rigid units.

Main Results:

  • Actin monomers (F-actin form) bound to both barbed and pointed ends of filaments with similar affinity.
  • Binding contacts and angles were consistent with existing structural data.
  • G-actin did not bind the pointed end, suggesting an activation barrier, but did bind the barbed end.

Conclusions:

  • Simulations provide insights into the kinetic pathways of actin filament nucleation and polymerization.
  • The flexibility of the D-loop influences binding angles at filament ends.
  • Identified non-productive binding configurations and potential areas for model refinement.