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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...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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...
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.
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...

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Updated: Jun 2, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

A model actin comet tail disassembling by severing.

P J Michalski1, A E Carlsson

  • 1Department of Physics, Washington University, St Louis, MO 63130, USA. pjmichal@physics.wustl.edu

Physical Biology
|May 14, 2011
PubMed
Summary
This summary is machine-generated.

This study models actin comet tail growth and disassembly using numerical simulations. The findings provide a formula to measure actin gel properties from tail dimensions, aiding research on cell motility.

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Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

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Last Updated: Jun 2, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Monitoring Actin Disassembly with Time-lapse Microscopy
06:12

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Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

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Area of Science:

  • Biophysics
  • Cell Biology
  • Computational Biology

Background:

  • Actin comet tails are propulsion structures in certain cells.
  • Understanding their dynamics is crucial for cell motility research.
  • Previous models lacked detailed quantitative predictions.

Purpose of the Study:

  • To develop a numerical model for actin comet tail formation and disassembly.
  • To investigate how bead properties and severing rates influence tail morphology.
  • To establish a method for inferring actin gel properties from macroscopic tail measurements.

Main Methods:

  • Numerical simulation of actin comet tail growth from a bead.
  • Modeling of tail disassembly via severing.
  • Analysis of macroscopic properties (radius, length) dependence on control parameters (bead diameter, velocity, severing rate, mesh size).

Main Results:

  • Predicted F-actin density profile: initial exponential decay followed by abrupt edge decay.
  • Predicted constant comet tail diameter along its length.
  • Developed a formula relating comet tail length to control parameters.

Conclusions:

  • The model accurately predicts actin comet tail structure and dynamics.
  • The derived formula allows quantitative assessment of actin gel mesh size and severing kinetics.
  • This approach offers a novel method for studying cellular propulsion mechanisms.