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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...
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...
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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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...
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 3, 2026

In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles
10:19

In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles

Published on: August 25, 2022

Divalent cation induced actin ring formation.

Harsimran Kaur1, Suresh Kumar, Kashmir Singh

  • 1Senior Research Fellow (SRF), Biomolecular Electronics and Nanotechnology Division (BEND), Central Scientific Instruments Organization (CSIO), Chandigarh, India. microsimbac@yahoo.co.in

International Journal of Biological Macromolecules
|March 15, 2011
PubMed
Summary
This summary is machine-generated.

Copper sulfate significantly alters actin filament structure, inducing branching, Y- and V-shapes, and ring formations at higher concentrations. This highlights the impact of divalent cations on actin morphology.

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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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In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles
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Published on: August 25, 2022

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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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

Area of Science:

  • Biochemistry
  • Cell Biology
  • Materials Science

Background:

  • Actin filaments are crucial cytoskeletal components.
  • Their morphology is sensitive to environmental conditions and ion concentrations.

Purpose of the Study:

  • To investigate the impact of copper sulfate on actin filament morphology.
  • To understand the role of divalent cations in altering actin structure.

Main Methods:

  • Incubation of actin filaments with varying concentrations of copper sulfate (2-5 mM).
  • Microscopic observation of morphological changes over time (4h and 8h).
  • Estimation of electrostatic adhesion energy.

Main Results:

  • Observed morphological changes including lateral branches, Y- and V-shapes at 2 mM copper sulfate.
  • Formation of rings and loops at 5 mM copper sulfate.
  • Actin ring formation was also induced in bead-tailed actin filaments.

Conclusions:

  • High concentrations of divalent cations like copper sulfate induce significant changes in actin filament morphology.
  • The polyelectrolyte nature of actin filaments contributes to these cation-induced structural alterations.
  • Actin ring formation exhibits similarities to DNA toroids but with greater bending stiffness.