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Related Concept Videos

Actin Treadmilling01:18

Actin Treadmilling

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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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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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Predator-Prey Interactions02:39

Predator-Prey Interactions

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Predators consume prey for energy. Predators that acquire prey and prey that avoid predation both increase their chances of survival and reproduction (i.e., fitness). Routine predator-prey interactions elicit mutual adaptations that improve predator offenses, such as claws, teeth, and speed, as well as prey defenses, including crypsis, aposematism, and mimicry. Thus, predator-prey interactions resemble an evolutionary arms race.
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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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Related Experiment Video

Updated: Feb 8, 2026

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium
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Actin dynamics in host-pathogen interaction.

Theresia E B Stradal1, Mario Schelhaas2

  • 1Department of Cell Biology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany.

FEBS Letters
|June 24, 2018
PubMed
Summary
This summary is machine-generated.

Pathogens target the actin cytoskeleton and Rho GTPase signaling, essential for cell processes like motility and autophagy. This review highlights pathogen-hijacked actin structures and future research directions.

Keywords:
actin dynamicsbacterial invasionhost-pathogen interactionviral entryvirulence factors

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Area of Science:

  • Cell Biology
  • Microbiology
  • Biochemistry

Background:

  • The actin cytoskeleton is crucial for fundamental cellular processes, including membrane remodeling, trafficking, and motility.
  • Rho GTPases are key regulators of actin assembly and dynamics.
  • Bacterial and viral pathogens frequently exploit the host cell's actin cytoskeleton for their life cycles.

Purpose of the Study:

  • To provide an overview of prominent pathogen-induced or -hijacked actin structures.
  • To explore the sophisticated interactions between pathogens and the host actin cytoskeleton.
  • To offer an outlook on future research in this field.

Main Methods:

  • Literature review of existing research on pathogen-actin interactions.
  • Analysis of documented pathogen-induced actin rearrangements.
  • Synthesis of current knowledge and identification of research gaps.

Main Results:

  • Pathogens manipulate actin for entry, replication, and egress.
  • Diverse actin structures are formed or co-opted by various pathogens.
  • Rho GTPase signaling pathways are frequently subverted by pathogens.

Conclusions:

  • The actin cytoskeleton is a central hub for pathogen manipulation.
  • Understanding these interactions is vital for developing novel therapeutic strategies.
  • Future research will likely reveal more intricate pathogen-host actin crosstalk.