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Related Concept Videos

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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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

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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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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Generation of Straight or Branched Actin Filaments01:14

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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

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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.
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Crystal structure of Anopheles gambiae actin depolymerizing factor explains high affinity to monomeric actin.

Devaki Lasiwa1, Inari Kursula1,2

  • 1Faculty of Biochemistry and Molecular Medicine, University of Oulu, Finland.

The FEBS Journal
|February 11, 2025
PubMed
Summary

Researchers determined the crystal structure of Anopheles gambiae actin-depolymerizing factor (AgADF), a protein crucial for malaria vector survival. This structure reveals conserved actin-binding sites and potential regulatory features, offering insights into parasite-host interactions.

Keywords:
PlasmodiumX‐ray crystallographyactin dynamicsisothermal titration calorimetryprotein–protein interaction

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Parasitology

Background:

  • Actin is a dynamic protein essential for cellular functions, regulated by actin-binding proteins.
  • Actin-depolymerizing factors (ADF)/cofilins are key regulators that accelerate actin turnover.
  • Malaria parasites (Plasmodium) require specific hosts, including the Anopheles mosquito vector, for their life cycle.

Purpose of the Study:

  • To determine the crystal structure of Anopheles gambiae ADF (AgADF).
  • To investigate the structural features of AgADF relevant to actin binding and regulation.
  • To provide insights into potential therapeutic targets within the malaria vector.

Main Methods:

  • X-ray crystallography was used to determine the AgADF structure.
  • Bio-physical techniques were employed to assess actin-binding affinity.
  • Sequence and structural comparisons were made with other ADF/cofilin proteins.

Main Results:

  • The crystal structure of AgADF reveals a conserved ADF/cofilin fold with characteristic β-strands, α-helices, and a β-hairpin loop.
  • Key G- and F-actin-binding sites are conserved in AgADF.
  • The structure suggests potential regulatory mechanisms involving membrane binding and redox state.
  • AgADF exhibits high-affinity binding (nanomolar Kd) to monomeric actin (ATP- and ADP-bound) and also binds actin filaments.

Conclusions:

  • The determined AgADF structure provides a detailed molecular understanding of this essential protein in the malaria vector.
  • Conserved actin-binding sites highlight potential conserved functions across species.
  • Identified regulatory features may offer novel avenues for targeting the malaria parasite's vector.