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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

6.9K
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...
6.9K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

4.0K
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...
4.0K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.8K
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...
3.8K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

7.1K
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....
7.1K
Actin Polymerization01:42

Actin Polymerization

8.9K
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...
8.9K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

4.1K
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...
4.1K

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Related Experiment Video

Updated: Mar 24, 2026

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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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

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Actin' like actin?

R D Mullins1, J F Kelleher, T D Pollard

  • 1Dept of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, 725 N. Wolfe St, Baltimore, MD 21205, USA.

Trends in Cell Biology
|June 1, 1996
PubMed
Summary
This summary is machine-generated.

Actin-related proteins (ARPs) are evolutionarily linked to actin and form the cell

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Last Updated: Mar 24, 2026

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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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Actin's self-association into microfilaments forms the essential cytoskeleton in eukaryotic cells.
  • This cytoskeleton is crucial for cell shape, mechanical properties, and motility.
  • Actin-related proteins (ARPs) are a recently discovered family sharing a common ancestor with actin.

Purpose of the Study:

  • To investigate the structural and functional relationships between conventional actin and ARPs.
  • To understand how ARPs interact with each other, actin, and actin-binding proteins.

Main Methods:

  • Comparative structural analysis based on atomic actin structures.
  • Modeling of ARP structures and interactions.

Main Results:

  • Three ubiquitous ARP classes share a common core structure with actin, including ATP-binding residues.
  • Divergence in surface residues suggests altered protein-protein interaction capabilities.
  • Structural models offer insights into ARP interactions.

Conclusions:

  • ARPs represent a diverse family with potential functional parallels to conventional actin.
  • Structural similarities and differences explain ARPs' distinct interaction profiles.
  • Further research into ARPs can elucidate cytoskeletal regulation and evolution.