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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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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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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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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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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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How distinct Arp2/3 complex variants regulate actin filament assembly.

Klemens Rottner1,2, Theresia E B Stradal1

  • 1Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.

Nature Cell Biology
|December 24, 2015
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Summary
This summary is machine-generated.

The Arp2/3 complex creates branched actin networks essential for cell movement and transport. Different Arp2/3 variants, alongside cortactin and coronin, regulate actin dynamics for diverse cellular functions.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • The Arp2/3 complex is a key regulator of actin cytoskeleton dynamics.
  • Actin networks drive crucial cellular processes including lamellipodium protrusion, vesicle trafficking, and pathogen motility.
  • Understanding the nuanced roles of Arp2/3 complex variants is vital for deciphering cellular mechanics.

Purpose of the Study:

  • To investigate the distinct functional roles of different Arp2/3 complex variants.
  • To elucidate how Arp2/3 complex variants interact with actin regulators like cortactin and coronin.
  • To understand the mechanisms by which Arp2/3 variants tune actin assembly and disassembly.

Main Methods:

  • Biochemical assays to analyze Arp2/3 complex activity.
  • In vitro reconstitution of actin filament networks.
  • Analysis of protein-protein interactions between Arp2/3 variants, cortactin, and coronin.

Main Results:

  • Demonstrated that distinct Arp2/3 complex variants exhibit differential regulation of actin filament branching.
  • Showed that cortactin and coronin modulate the activity of specific Arp2/3 variants.
  • Identified unique contributions of Arp2/3 variants in controlling actin assembly and disassembly rates.

Conclusions:

  • The Arp2/3 complex is not a monolithic entity but comprises variants with specialized functions.
  • Coordinated action of Arp2/3 variants with cortactin and coronin provides sophisticated control over actin dynamics.
  • These findings offer new insights into the regulation of cellular structures and motility.