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Related Concept Videos

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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...
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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.
Introduction to Actin01:26

Introduction to Actin

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 different species.
Actin Polymerization01:42

Actin Polymerization

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 actin...

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Related Experiment Video

Updated: Jul 6, 2026

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Characterization and expression of an actin-depolymerizing factor from Eimeria tenella.

Jia-Hua Xu1, Zhong-Hua Qin, Yu-Shen Liao

  • 1School of Life Sciences, Sun Yat-sen University, Guangzhou, Guangdong Province, China.

Parasitology Research
|April 15, 2008
PubMed
Summary

Eimeria tenella actin-depolymerizing factor (ADF) was identified and characterized. Its expression is highest in invasive stages, suggesting ADF is crucial for apicomplexan parasite host cell invasion.

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Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites
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Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites

Published on: February 14, 2020

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Last Updated: Jul 6, 2026

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites
08:26

Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites

Published on: February 14, 2020

Area of Science:

  • Parasitology
  • Molecular Biology
  • Cell Biology

Background:

  • Actin-depolymerizing factor (ADF) is vital for actin cytoskeleton remodeling.
  • Actin cytoskeleton dynamics are critical for host cell invasion by apicomplexan parasites.

Purpose of the Study:

  • To clone and characterize the Eimeria tenella ADF gene and protein.
  • To investigate the expression patterns of E. tenella ADF during its life cycle.
  • To assess the functional role of E. tenella ADF in actin binding.

Main Methods:

  • Gene cloning and sequencing using E. tenella genome data.
  • Bioinformatic analysis of the deduced amino acid sequence and protein structure.
  • Real-time RT-PCR, dot blot, and Northern blot for gene and protein expression analysis.
  • In vitro actin-binding assays with recombinant ADF protein.

Main Results:

  • The E. tenella ADF gene was cloned, encoding a 118-amino acid protein lacking signal or nuclear localization sequences.
  • E. tenella ADF shares 69.1% sequence similarity with Toxoplasma gondii ADF.
  • Structural comparison revealed potential differences in actin filament binding sites.
  • ADF expression (mRNA and protein) was significantly higher in sporozoites and merozoites compared to oocysts.
  • Northern blot confirmed a single ADF transcript form across all life stages.
  • Recombinant E. tenella ADF protein demonstrated actin-binding capability.

Conclusions:

  • Eimeria tenella ADF is a functional protein with conserved features and unique structural aspects.
  • ADF expression levels correlate with invasive parasite stages, highlighting its role in host cell invasion.
  • The actin-binding ability of E. tenella ADF supports its proposed function in parasite motility and invasion.