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Related Concept Videos

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
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...
5.2K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
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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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 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
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...
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Updated: Jul 2, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Nuclear actin filaments - a historical perspective.

Maria Kristha Fernandez1, Molika Sinha1, Mia Zidan1

  • 1Gynecologic Oncology Division, School of Medicine Stanford University, Palo Alto, CA, USA.

Nucleus (Austin, Tex.)
|February 22, 2024
PubMed
Summary

Nuclear actin filaments, once thought rare, are now recognized as crucial for chromatin organization, nuclear biomechanics, gene expression, and DNA repair in mammalian cells.

Keywords:
Biomechanics of cell nucleusDNA damage repairnuclear actin filamentsnucleocytoplasmic shuttlingsignaling and gene expression

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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos
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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
  • Biophysics

Background:

  • Nuclear actin filaments were initially observed in amphibian oocytes and under stress in mammalian cells.
  • Early observations were limited by labeling and imaging technologies.

Purpose of the Study:

  • To provide a historical perspective on the evolving understanding of nuclear actin filaments.
  • To highlight the functional significance of nuclear actin in mammalian cells.

Main Methods:

  • Historical review of scientific literature.
  • Analysis of advancements in cell imaging and labeling techniques.

Main Results:

  • Nuclear actin filaments form a transient network relevant to nuclear functions.
  • Key roles identified in chromatin organization, nuclear biomechanics, gene expression, and DNA repair.

Conclusions:

  • The perception of nuclear actin filaments has shifted from a rare phenomenon to a functionally significant component of the mammalian nucleus.
  • Ongoing technological advancements continue to reveal the dynamic roles of nuclear actin.