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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...
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.
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...
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...
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...
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...

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Related Experiment Video

Updated: May 15, 2026

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

Disulfide cross-linked antiparallel actin dimer.

Philip Graceffa1, Eunhee Lee, Walter F Stafford

  • 1Boston Biomedical Research Institute, Watertown, MA 02472, USA. graceffa@bbri.org

Biochemistry
|January 9, 2013
PubMed
Summary
This summary is machine-generated.

Oxidation of actin monomer (G-actin) rapidly forms antiparallel dimers via disulfide bonds. Actin polymer (F-actin) yields fewer dimers, suggesting they form during polymerization dynamics, not from stable dimers.

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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
08:02

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

Published on: May 5, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Dynamics

Background:

  • Actin is a crucial protein for cell structure and motility.
  • The formation and stability of actin dimers are key to understanding polymerization dynamics.
  • Previous models proposed stable antiparallel actin dimers as polymerization intermediates.

Purpose of the Study:

  • To investigate the mechanism of disulfide cross-linked actin dimer formation.
  • To differentiate between dimers formed from monomers versus those from polymers.
  • To re-evaluate the role of antiparallel actin dimers in polymerization models.

Main Methods:

  • Oxidation of G-actin and F-actin using copper o-phenanthroline.
  • Analytical ultracentrifugation to assess dimer presence and stability.
  • Analysis of disulfide bond formation at Cys374.

Main Results:

  • Rapid, high yield of disulfide cross-linked antiparallel actin dimers from G-actin via random collisions.
  • Lower yield of cross-linked dimers from F-actin, with no leveling off, suggesting formation from dynamic polymerization equilibria.
  • Cross-linked dimer formation correlates with actin monomer concentration during polymerization.

Conclusions:

  • Disulfide cross-linked antiparallel actin dimers are primarily formed from monomeric actin (G-actin) through diffusion.
  • Dimers from polymerized actin (F-actin) likely arise from transient monomeric species during treadmilling.
  • The formation of cross-linked dimers does not necessarily imply the existence of stable, pre-formed actin dimers.