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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...
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...
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...
Actin Treadmilling01:18

Actin Treadmilling

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...
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.
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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.

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Related Experiment Video

Updated: May 19, 2026

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

History-dependent depolymerization of actin filaments.

Ishutesh Jain1, David Lacoste, Dulal Panda

  • 1Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.

Biochemistry
|September 1, 2012
PubMed
Summary
This summary is machine-generated.

Polymerization history affects how actin filaments depolymerize and fluctuate in length. This study reveals distinct depolymerization regimes under constant concentration and mass conservation conditions.

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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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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Last Updated: May 19, 2026

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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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

Published on: May 5, 2022

Area of Science:

  • Cellular biology
  • Biophysics
  • Cytoskeletal dynamics

Background:

  • Cytoskeletal filaments, such as actin, are crucial for fundamental cellular processes like division and motility.
  • Understanding filament depolymerization is as critical as understanding polymerization for cell function.
  • Nonequilibrium dynamics of cytoskeletal components are key to cellular mechanics.

Purpose of the Study:

  • To investigate the nonequilibrium depolymerization of actin filaments.
  • To elucidate the influence of polymerization history on depolymerization dynamics and length fluctuations.
  • To simulate and characterize depolymerization under experimentally relevant conditions.

Main Methods:

  • Utilized a simplified two-state model for actin filament depolymerization.
  • Simulated depolymerization processes under controlled conditions.
  • Analyzed depolymerization dynamics and length fluctuations.

Main Results:

  • Demonstrated that the history of actin filament polymerization impacts subsequent depolymerization dynamics.
  • Observed that polymerization history also affects length fluctuations during depolymerization.
  • Identified two distinct depolymerization regimes under constant concentration conditions.
  • Revealed the possibility of three depolymerization regimes under mass-conserving conditions.

Conclusions:

  • Actin filament depolymerization is not solely dependent on current conditions but is significantly influenced by its polymerization history.
  • The observed depolymerization regimes provide insights into the complex behavior of cytoskeletal dynamics in living cells.
  • This research offers a foundation for further experimental and theoretical studies on cytoskeletal filament dynamics.