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Related Concept Videos

Actin Treadmilling01:18

Actin Treadmilling

9.7K
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...
9.7K
Introduction to Actin01:26

Introduction to Actin

6.6K
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...
6.6K
Actin Polymerization01:42

Actin Polymerization

8.6K
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...
8.6K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.9K
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...
3.9K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.6K
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...
3.6K
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

4.9K
Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Related Experiment Video

Updated: Feb 2, 2026

Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
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Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons

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Actin Microridges.

Joseph A Depasquale1

  • 1Morphogenyx Inc, East Northport, New York.

Anatomical Record (Hoboken, N.J. : 2007)
|November 11, 2018
PubMed
Summary

Microridges, actin-based epithelial structures, are widespread but understudied. Further research into their molecular composition and function is needed, especially concerning their role in health and disease.

Area of Science:

  • Cell Biology
  • Epithelial Biology
  • Cytoskeletal Dynamics

Background:

  • Microridges are distinctive, fingerprint-patterned structures on epithelial cell surfaces.
  • These structures are primarily composed of an F-actin cytoskeleton.
  • Existing research predominantly utilizes fish epithelial models, with limited comparative studies across species.

Purpose of the Study:

  • To provide a comprehensive overview of microridges by integrating knowledge from fish and mammalian studies.
  • To highlight the underrepresentation of microridge research compared to other actin-based cellular structures.
  • To emphasize the potential significance of microridges in both healthy physiological conditions and disease states.

Main Methods:

  • Literature review integrating studies from fish and mammalian species.
Keywords:
actin microridgesfish epidermismicroplicae

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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

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Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin
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Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

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Related Experiment Videos

Last Updated: Feb 2, 2026

Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons
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Quantification of Filamentous Actin F-actin Puncta in Rat Cortical Neurons

Published on: February 10, 2016

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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

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Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin
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Study of the Actin Cytoskeleton in Live Endothelial Cells Expressing GFP-Actin

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  • Comparative analysis of microridge research volume against other actin-based structures (e.g., lamellipodia, filopodia).
  • Examination of PubMed search data for relevant keywords: "Microridges," "Microplicae," and "Actin Microridges."

    • Main Results:

    • Microridges are ubiquitous across various species and tissues, yet their study is limited.
    • Literature on microridges is significantly smaller than for other actin-based structures involved in cell motility.
    • Molecular composition and functional roles of microridges remain largely unclear.

    Conclusions:

    • The widespread distribution of microridges suggests fundamental roles in healthy organisms.
    • Alterations in microridge structure and function may serve as indicators of disease.
    • Further in-depth investigation into microridge molecular makeup and physiological functions is warranted.