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Related Concept Videos

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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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Formation of Higher-order Actin Filaments01:11

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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...
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Studying the Cytoskeleton01:17

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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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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...
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Related Experiment Video

Updated: Nov 15, 2025

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

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F-actin Bundle Sedimentation Assay.

Shan-Shan Lin1, Mei-Chun Chuang1, Ya-Wen Liu1,2

  • 1Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan.

Bio-Protocol
|March 3, 2021
PubMed
Summary
This summary is machine-generated.

This study presents a simple in vitro protocol to analyze actin bundling activity. It uses the large GTPase, dynamin, as an example to quantify how proteins cross-link and bundle actin filaments.

Keywords:
Actin bundleActin crosslinkerDynaminGTPaseInvadosome

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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

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Related Experiment Videos

Last Updated: Nov 15, 2025

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

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Measuring Protein Binding to F-actin by Co-sedimentation
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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

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Cell biology

Background:

  • Understanding higher-order regulation of actin dynamics is crucial.
  • Dynamin, a membrane-remodeling GTPase, is a newly identified actin cross-linking molecule.
  • Dynamin influences the actin cytoskeleton by binding, self-assembling around, and bundling actin filaments.

Purpose of the Study:

  • To present a simple, quantitative in vitro protocol for analyzing actin bundling activity.
  • To use dynamin as a model protein to demonstrate the protocol.
  • To provide a method applicable to other actin-binding proteins.

Main Methods:

  • F-actin reconstitution.
  • Quantitative analysis of actin bundling.
  • Qualitative analysis of actin bundling.

Main Results:

  • A straightforward protocol for assessing actin bundling activity was established.
  • The protocol successfully demonstrated the actin bundling capabilities of dynamin.
  • The method allows for both qualitative and quantitative measurements.

Conclusions:

  • The developed protocol provides a valuable tool for studying actin-binding proteins.
  • This assay facilitates a deeper understanding of actin cytoskeleton regulation.
  • The protocol is adaptable for analyzing the bundling activity of various actin-binding proteins.