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Related Concept Videos

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.0K
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...
3.0K
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...
2.9K
Introduction to Actin01:26

Introduction to Actin

4.9K
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...
4.9K
Actin Treadmilling01:18

Actin Treadmilling

7.9K
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...
7.9K
Actin Polymerization01:42

Actin Polymerization

6.3K
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...
6.3K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

2.9K
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...
2.9K

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Related Experiment Video

Updated: May 31, 2025

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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Structural insights into actin filament turnover.

Wout Oosterheert1, Micaela Boiero Sanders1, Peter Bieling2

  • 1Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany.

Trends in Cell Biology
|January 23, 2025
PubMed
Summary
This summary is machine-generated.

Actin filament dynamics, crucial for cell movement, are detailed through structural insights. This review covers actin polymerization, aging, barbed-end growth regulation, and pointed-end disassembly mechanisms.

Keywords:
actinbarbed endcytoskeletonfilament turnoverpointed endstructural biology

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • Actin filaments are essential for eukaryotic cell morphogenesis and migration.
  • Understanding actin dynamics is key to deciphering fundamental cellular processes.

Purpose of the Study:

  • To review recent structural insights into actin polymerization and disassembly mechanisms.
  • To elucidate the molecular regulation of actin filament dynamics.

Main Methods:

  • High-resolution structural analysis of actin filament assemblies.
  • Review of literature on actin dynamics and regulation.

Main Results:

  • Actin subunits undergo aging within filaments via nucleotide changes.
  • Profilin, formin, and capping protein (CP) modulate barbed-end growth.
  • Cofilin/cyclase-associated protein (CAP) and DNase I mediate pointed-end depolymerization.

Conclusions:

  • Structural understanding reveals mechanisms of actin filament turnover.
  • Regulation of actin dynamics is complex and finely tuned in cellular environments.