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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 Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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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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Introduction to Actin01:26

Introduction to Actin

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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 Filament Depolymerization01:19

Actin Filament Depolymerization

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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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Actin Polymerization01:42

Actin Polymerization

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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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Related Experiment Video

Updated: Jan 10, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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A microexon in Arp2 alters tissue-specific Arp2/3-generated actin structures.

Jordan Powell1, Manuela Sophia Palafox1, Courtney M Schroeder1

  • 1Department of Pharmacology, UT Southwestern Medical Center, Dallas, TX.

Biorxiv : the Preprint Server for Biology
|November 24, 2025
PubMed
Summary

The Arp2/3 complex subunit Arp2 has two splice variants, Arp2L and Arp2s. While functionally similar in vitro, Arp2L causes sperm defects in vivo, yet offers an evolutionary fitness advantage.

Keywords:
Arp2/3actincytoskeletonevolutionmicroexonsperm developmentsplice variants

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Micromanipulation Techniques Allowing Analysis of Morphogenetic Dynamics and Turnover of Cytoskeletal Regulators
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Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Evolutionary Biology

Background:

  • The Arp2/3 complex is crucial for branched actin networks in eukaryotes.
  • The Arp2 gene encodes two splice variants differing by a microexon in the actin-binding D-loop.

Purpose of the Study:

  • To investigate the expression and function of Drosophila Arp2 splice variants.
  • To determine if the Arp2 microexon impacts Arp2/3 complex function in vitro and in vivo.

Main Methods:

  • Expressed and purified recombinant Drosophila Arp2/3 complexes with Arp2s and Arp2L variants.
  • Generated Drosophila melanogaster lines with Arp2s or Arp2L replacing endogenous Arp2.
  • Assessed actin polymerization in vitro and sperm development phenotypes in vivo.

Main Results:

  • The Arp2 microexon is evolutionarily conserved but varies in sequence.
  • Both Arp2s and Arp2L variants rescue Arp2 knockout lethality in Drosophila.
  • Arp2L expression leads to defects in sperm actin cone alignment and motility, independent of D-loop length.

Conclusions:

  • Drosophila Arp2 splice variants are non-redundant in vivo, with Arp2L specialized for tissue-specific roles.
  • The Arp2 microexon sequence, not just length, drives functional divergence.
  • Despite tissue-specific costs, Arp2L confers an overall evolutionary fitness advantage.