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Related Concept Videos

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...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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...
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...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

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Related Experiment Video

Updated: Jun 14, 2026

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

Actin filament remodeling by actin depolymerization factor/cofilin.

Jim Pfaendtner1, Enrique M De La Cruz, Gregory A Voth

  • 1Department of Chemical Engineering, University of Washington, Box 351750, Seattle, WA 98195-1750, USA.

Proceedings of the National Academy of Sciences of the United States of America
|April 7, 2010
PubMed
Summary
This summary is machine-generated.

Actin depolymerization factor (ADF)/cofilin binding alters actin filament structure and dynamics. This interaction weakens subunit connections, reducing filament bending rigidity and providing molecular insights into actin allostery.

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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:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Actin filaments are crucial cytoskeletal components involved in cell motility and structure.
  • Actin depolymerization factor (ADF)/cofilin is a key protein regulating actin dynamics.
  • Understanding ADF/cofilin's precise mechanism on actin structure is essential.

Purpose of the Study:

  • To investigate how ADF/cofilin binding affects actin filament structure, dynamics, and mechanical properties.
  • To elucidate the molecular basis of actin filament allostery and its connection to ADF/cofilin.

Main Methods:

  • All-atom molecular dynamics simulations.
  • Analysis of thermal fluctuations in actin filament shape.
  • Investigation of actin and cofilactin filament bending stiffness and persistence lengths.

Main Results:

  • ADF/cofilin binding alters actin filament flexibility by repositioning the DNase-I binding loop.
  • Filament bending rigidity is reduced due to weakened subunit interactions along the long-pitch helix.
  • Lateral filament contacts are compromised, impacting overall filament stability.

Conclusions:

  • ADF/cofilin binding significantly impacts actin filament mechanical properties by disrupting inter-subunit interactions.
  • The study reveals the molecular mechanisms underlying actin filament allostery and its regulation by ADF/cofilin.