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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

5.1K
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

6.6K
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...
6.6K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.2K
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....
5.2K
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
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
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...
2.9K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K

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Related Experiment Video

Updated: Jun 29, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Nuclear actin dynamics and functions at a glance.

Svenja Ulferts1, Massimo Lopes2, Kei Miyamoto3

  • 1Institute for Clinical and Experimental Pharmacology and Toxicology I, Medical Faculty, University of Freiburg, 79104 Freiburg, Germany.

Journal of Cell Science
|April 2, 2024
PubMed
Summary

Nuclear actin filaments regulate genome functions, including cell cycle, DNA repair, and chromatin organization. These dynamics are crucial for meiosis and embryonic development.

Keywords:
Chromatin dynamicsDNA damageDNA repairNuclear actinNuclear architectureOocyte developmentTranscription

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

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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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Related Experiment Videos

Last Updated: Jun 29, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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

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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
  • Molecular Biology
  • Genomics

Background:

  • Actin's primary role is in the cytoskeleton, maintaining cell shape and enabling migration.
  • Nuclear actin is increasingly recognized for its involvement in genome regulation.
  • Advances in imaging reveal dynamic nuclear actin filament formation.

Purpose of the Study:

  • To summarize signaling pathways that drive nuclear actin filament assembly.
  • To elucidate the roles of nuclear actin in genome functions.
  • To highlight the physiological importance of nuclear actin in reproduction.

Main Methods:

  • Review of signaling events.
  • Analysis of microscopy and imaging data.
  • Literature synthesis on nuclear actin functions.

Main Results:

  • Nuclear actin filaments assemble dynamically, influenced by specific signaling pathways.
  • Nuclear actin is integral to chromatin remodeling, cell cycle control, DNA replication/repair, and transcriptional condensate formation.
  • Specific roles in meiosis and early embryonic development are identified.

Conclusions:

  • Nuclear actin dynamics are essential for fundamental genome processes.
  • Nuclear actin plays critical roles beyond its cytoskeletal functions.
  • Further research into nuclear actin signaling promises insights into development and disease.