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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

5.2K
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 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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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

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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Studying the Cytoskeleton01:17

Studying the Cytoskeleton

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The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
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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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Updated: Jul 28, 2025

Analyzing the α-Actinin Network in Human iPSC-Derived Cardiomyocytes Using Single Molecule Localization Microscopy
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A deep learning framework for quantitative analysis of actin microridges.

Rajasekaran Bhavna1,2, Mahendra Sonawane3

  • 1Department of Biological Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai, 400005, India. bhavnarajasekaran@yahoo.com.

NPJ Systems Biology and Applications
|June 2, 2023
PubMed
Summary
This summary is machine-generated.

Researchers developed a deep learning method to analyze microridges, revealing their mechanical properties and distinct actomyosin network regulation in zebrafish epidermal cells. This offers new insights into epithelial development and patterning mechanisms.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Developmental Biology

Background:

  • Microridges are actin-rich cell surface protrusions on squamous epithelia.
  • Their dynamic patterns in zebrafish are driven by actomyosin networks but poorly understood.
  • Existing computational methods limit quantitative analysis.

Purpose of the Study:

  • To develop a computational framework for analyzing microridge morphology and dynamics.
  • To quantitatively investigate the bio-physical-mechanical characteristics of microridges.
  • To understand the role of actomyosin networks in microridge pattern formation.

Main Methods:

  • A deep learning strategy for high-accuracy microridge segmentation (~95% pixel-level).
  • Estimation of effective microridge persistence length from segmented images.
  • Analysis of mechanical fluctuations and stored stresses within microridge patterns.

Main Results:

  • Quantified microridge characteristics, estimating an effective persistence length of ~6.1 μm.
  • Identified distinct actomyosin network regulation between yolk and flank epithelial cells based on stored stresses.
  • Observed spontaneous actin cluster dynamics linked to pattern rearrangements.

Conclusions:

  • The developed deep learning framework enables large-scale spatiotemporal analysis of microridges.
  • Insights into microridge mechanics and actomyosin network regulation during epithelial development.
  • Provides a tool to probe microridge responses to genetic and chemical perturbations.