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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 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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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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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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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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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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Updated: Feb 23, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Bin1 directly remodels actin dynamics through its BAR domain.

Nina M Dräger1, Eliana Nachman1,2, Moritz Winterhoff3

  • 1Proteostasis in Neurodegenerative Disease (B180), Schaller Research Group at the University of Heidelberg and DKFZ, Heidelberg, Germany.

EMBO Reports
|September 13, 2017
PubMed
Summary

Bin1 protein shapes cell membranes and binds actin, stabilizing filaments. This protein

Keywords:
Alzheimer's diseaseN‐BAR protein Bin1actin bindinggenetic risk factortau

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Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • Endocytic processes rely on BAR-domain proteins and actin polymerization.
  • Bin1, an N-BAR protein, senses and curves membranes.
  • Bin1 is a risk factor for Alzheimer's disease, but its role in neurodegeneration is unclear.

Purpose of the Study:

  • To investigate Bin1's role in actin binding and dynamics.
  • To explore Bin1's involvement in Alzheimer's disease pathology.

Main Methods:

  • Investigated human Bin1's actin bundling and filament stabilization activities.
  • Examined Bin1's effect on tau-induced actin bundles.
  • Utilized a Drosophila model of tauopathy to assess Bin1's in vivo function.

Main Results:

  • Bin1 binds actin via its BAR domain and exhibits moderate actin bundling activity.
  • Bin1 stabilizes actin filaments against depolymerization.
  • Bin1 stabilizes tau-induced actin bundles, and its downregulation reduces tau-induced actin inclusions in a Drosophila model.

Conclusions:

  • Bin1 modifies actin dynamics, suggesting a mechanistic link to tau-induced pathobiological changes.
  • Bin1's actin-binding and stabilizing properties may contribute to its role in Alzheimer's disease pathogenesis.