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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.6K
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...
3.6K
Introduction to Actin01:26

Introduction to Actin

6.2K
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...
6.2K
Actin Polymerization01:42

Actin Polymerization

8.2K
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...
8.2K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.5K
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...
3.5K
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

8.4K
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...
8.4K
Actin Treadmilling01:18

Actin Treadmilling

9.4K
Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
9.4K

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Related Experiment Video

Updated: Jan 7, 2026

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

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

798

Nucleotide-dependent actin conformations revealed by multiscale enhanced sampling.

Kenta Omoto1, Ryotato Koike2, Kei Moritsugu1

  • 1Graduate School of Science, Osaka Metropolitan University, 1-2 Gakuencho, Naka-ku, Sakai, Osaka 599-8570, Japan.

Biophysical Journal
|December 7, 2025
PubMed
Summary
This summary is machine-generated.

Actin filament growth is directional due to nucleotide binding. ATP-bound actin monomers favor barbed end addition, while ADP-bound actin favors pointed end dissociation, explaining filament polarity.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Actin filaments form the cytoskeleton, crucial for cell motility and transport.
  • Filament polarity (barbed/plus and pointed/minus ends) dictates directional growth.
  • Nucleotide state (ATP vs. ADP) regulates actin dynamics.

Purpose of the Study:

  • To investigate the conformational dynamics of G-actin and F-actin with bound ATP or ADP.
  • To elucidate the molecular mechanisms underlying nucleotide-dependent actin filament polarity and growth.

Main Methods:

  • Multiscale enhanced sampling simulations for conformational analysis.
  • Utilized high-resolution crystal structures of actin-binding protein complexes.
  • Performed atom contact analysis to identify key interactions.

Main Results:

  • ATP-bound G-actin shows greater flexibility, favoring filament association.
  • ADP-bound F-actin exhibits increased flexibility, promoting dissociation from the pointed end.
  • Nucleotide-dependent conformational changes explain the directional growth of actin filaments.

Conclusions:

  • The study explains actin filament's directional growth based on nucleotide state.
  • ATP binding enhances G-actin's ability to join the filament barbed end.
  • ADP binding promotes F-actin's dissociation from the filament pointed end.