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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

5.1K
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...
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Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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....
5.2K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
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...
3.0K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.1K
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...
3.1K
Actin Polymerization01:42

Actin Polymerization

6.6K
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...
6.6K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
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: Jun 28, 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

Published on: March 28, 2008

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BioID Analysis of Actin-Binding Proteins.

E Emily Joo1, Michael F Olson2

  • 1Department of Chemistry and Biology, Toronto Metropolitan University, Toronto, ON, Canada.

Methods in Molecular Biology (Clifton, N.J.)
|April 17, 2024
PubMed
Summary

Researchers developed a new method using TurboID and LifeAct to identify proteins interacting with actin. This technique allows for rapid comparison of actin-binding proteins under various cellular conditions.

Keywords:
ActinAffinity purificationBiotin ligaseCytoskeletonLifeActProximity ligation

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Measuring Protein Binding to F-actin by Co-sedimentation
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Measuring Protein Binding to F-actin by Co-sedimentation

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Related Experiment Videos

Last Updated: Jun 28, 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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Measuring Protein Binding to F-actin by Co-sedimentation
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Measuring Protein Binding to F-actin by Co-sedimentation

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Proteomics

Background:

  • Proteins function within complexes and networks, making it challenging to identify interacting partners.
  • Understanding protein proximity is crucial for deciphering cellular functions and pathways.

Purpose of the Study:

  • To develop a method for identifying proteins proximal or bound to actin.
  • To leverage the rapid kinetics of TurboID for dynamic studies of actin-binding proteins.

Main Methods:

  • Fusion of the promiscuous biotin ligase TurboID to the actin-binding peptide LifeAct.
  • Biotinylation of proteins in close proximity to actin.
  • Comparison of actin-binding protein profiles under normal and disrupted filamentous actin conditions (using cytochalasin D).

Main Results:

  • Successfully labeled proteins in close proximity to actin using the TurboID-LifeAct fusion.
  • Demonstrated the ability to compare actin-binding protein profiles under different cellular conditions.
  • The rapid enzyme kinetics of TurboID enabled efficient labeling and comparison.

Conclusions:

  • The TurboID-LifeAct system is an effective tool for identifying actin-interacting proteins.
  • This method facilitates the study of dynamic changes in protein-protein interactions related to actin.
  • Enables comprehensive analysis of the actin interactome under various physiological or experimental conditions.