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Related Concept Videos

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...
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...
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...
Actin Filament Depolymerization01:19

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...
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.

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Related Experiment Video

Updated: Jun 14, 2026

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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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

Antiparallel dimer and actin assembly.

Elena E Grintsevich1, Martin Phillips, Dmitry Pavlov

  • 1Department of Chemistry and Biochemistry and Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.

Biochemistry
|April 6, 2010
PubMed
Summary
This summary is machine-generated.

Novel tools reveal that antiparallel dimers (APDs) transiently incorporate into actin filaments, inhibiting polymerization. This study offers new methods to examine APD effects under physiological conditions.

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Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
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Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Published on: July 12, 2022

Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • The antiparallel dimer (APD) is a critical actin species observed during early polymerization stages.
  • Understanding APD's role requires effective detection and monitoring tools.

Purpose of the Study:

  • To introduce novel tools for examining APD effects on actin polymerization.
  • To characterize APD formation, stability, and kinetics under physiological conditions.
  • To investigate APD's influence on actin nucleation and filament elongation.

Main Methods:

  • Utilized bifunctional methanothiosulfonate (MTS) reagents for APD detection and cross-linking.
  • Employed pyrene-labeled yeast actin mutant (C167PM) to form and monitor stable APDs in solution.
  • Conducted sedimentation equilibrium experiments to characterize C167PM dimerization.
  • Analyzed APD decay kinetics relative to filament elongation rates.

Main Results:

  • MTS reagents provide efficient APD detection at neutral pH, outperforming p-phenylene maleimide (pPDM).
  • C167PM actin forms stable APDs in solution, allowing kinetic monitoring without external agents.
  • APD dimerization exhibits a dissociation constant (K(d)) of approximately 0.3 microM.
  • APD decay occurs slower than filament elongation, indicating transient incorporation.
  • APD formation inhibits both nucleation and elongation of actin filaments.

Conclusions:

  • A novel system using C167PM actin enables APD assessment under physiological conditions.
  • The APD is a transient species that plays an inhibitory role in actin polymerization.
  • Bifunctional MTS reagents are effective alternatives for APD detection in actin research.