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Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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...
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Actin Filament Depolymerization01:19

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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...
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Introduction to Actin01:26

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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...
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Actin Polymerization01:42

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

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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...
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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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...
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Related Experiment Video

Updated: May 2, 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

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Dissecting principles governing actin assembly using yeast extracts.

Alphée Michelot1, David G Drubin2

  • 1Physics of the Cytoskeleton and Morphogenesis Group, institut de Recherches en Technologies et Sciences pour le Vivant, iRTSV, LPCV/CNRS/CEA/INRA/UJF, Grenoble, France.

Methods in Enzymology
|March 18, 2014
PubMed
Summary

Researchers developed new protocols for actin assembly and motility in yeast cell extracts. This method enables rapid preparation of yeast extracts for studying actin dynamics and protein functions in various cellular contexts.

Keywords:
ActinArp2/3AssayExtractForminNucleationWASP

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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Actin assembly and motility are fundamental cellular processes.
  • Studying these processes in cell extracts offers a controlled environment.
  • Yeast provides a powerful system for genetic manipulation and reconstituted assays.

Purpose of the Study:

  • To describe novel protocols for triggering actin assembly and motility in yeast cell extracts.
  • To enable the fast preparation of yeast extracts for dynamic actin filament studies.
  • To facilitate the dissection of individual protein functions in reconstituted systems.

Main Methods:

  • Development of protocols for rapid yeast extract preparation.
  • Utilizing yeast cell extracts for actin assembly and motility assays.
  • Employing systems of variable complexity for protein activity analysis.

Main Results:

  • Successfully triggered actin assembly and actin-based motility in yeast extracts.
  • Prepared yeast extracts competent for dynamic assembly of actin filament structures.
  • Demonstrated the advantage of yeast for combining reconstituted assays with genetic modifications.

Conclusions:

  • The developed protocols offer a robust method for studying actin dynamics in yeast.
  • Yeast cell extracts provide a versatile platform for dissecting protein functions in actin-based processes.
  • This approach allows for analysis across a spectrum of biological complexity, from purified proteins to whole cell extracts.