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Related Concept Videos

Actin Polymerization01:42

Actin Polymerization

6.7K
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...
6.7K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.3K
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....
5.3K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.1K
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...
3.1K
Actin Treadmilling01:18

Actin Treadmilling

8.1K
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...
8.1K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

2.6K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.6K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.4K
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...
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Related Experiment Video

Updated: Jul 15, 2025

Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Actin polymerization and depolymerization in developing vertebrates.

Yang Bai1,2,3, Feng Zhao1,2,3, Tingting Wu1,2,3

  • 1Stomatological Hospital of Chongqing Medical University, Chongqing, China.

Frontiers in Physiology
|September 25, 2023
PubMed
Summary
This summary is machine-generated.

Actin polymerization is crucial for embryonic development, tissue formation, and organogenesis. Understanding actin dynamics can lead to new therapies for developmental disorders and tissue regeneration.

Keywords:
F-actinG-actinembryonic developmentmorphogenesisorganogenesis

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In Vitro Polymerization of F-actin on Early Endosomes
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In Vitro Polymerization of F-actin on Early Endosomes

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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

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In Vitro Polymerization of F-actin on Early Endosomes
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Area of Science:

  • Cell Biology
  • Developmental Biology
  • Biochemistry

Background:

  • Filamentous actin (F-actin) is a key cytoskeletal component vital for cellular and tissue morphogenesis during development.
  • The dynamic equilibrium between globular actin (G-actin) polymerization and depolymerization is essential for normal cellular function.
  • Imbalances in actin dynamics can cause developmental abnormalities, defects, and embryonic lethality.

Purpose of the Study:

  • To review recent findings on G-actin and F-actin structures and polymerization.
  • To explore the functions of different actin isoforms.
  • To elucidate the mechanisms of actin polymerization/depolymerization in developmental morphogenesis.

Main Methods:

  • Literature review of recent research findings.
  • Analysis of actin structure and polymerization dynamics.
  • Focus on cellular and organic morphogenesis.

Main Results:

  • Detailed review of G-actin and F-actin structures.
  • Exploration of actin polymerization mechanisms.
  • Emphasis on the role of actin dynamics in morphogenesis.

Conclusions:

  • Understanding actin polymerization is vital for comprehending physiological and pathological processes in development.
  • This knowledge may pave the way for novel therapeutics targeting embryonic developmental abnormalities.
  • Insights into actin dynamics could advance tissue regeneration strategies.