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Related Concept Videos

Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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....
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Introduction to Actin01:26

Introduction to Actin

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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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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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Actin Polymerization01:42

Actin Polymerization

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

The Role of Actin and Myosin in Non-muscle Cells

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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: Mar 14, 2026

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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Nucleus-associated actin in Amoeba proteus.

Mariia Berdieva1, Dmitry Bogolyubov1, Yuliya Podlipaeva1

  • 1Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Avenue, 194064 St. Petersburg, Russia.

European Journal of Protistology
|September 30, 2016
PubMed
Summary

Actin is abundant in the Amoeba proteus nucleus, primarily as G-actin associated with chromatin. This finding supports actin's role in fundamental nuclear processes across diverse organisms.

Keywords:
Amoeba proteusImmunocytochemistryNuclear actinNucleus

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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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Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics
  • Molecular Biology

Background:

  • Actin, a key cytoskeletal protein, is traditionally associated with cytoplasmic functions.
  • Its presence and role within the nucleus are increasingly recognized but not fully elucidated in unicellular organisms.

Purpose of the Study:

  • To investigate the presence, distribution, and forms of actin within the nucleus and associated cytoplasm of Amoeba proteus.
  • To explore the potential architectural function of nuclear-associated actin.

Main Methods:

  • Immunocytochemical approaches using anti-actin antibodies.
  • Staining with TRITC-phalloidin and fluorescent deoxyribonuclease I (DNase I).
  • Treatment with the actin-depolymerizing agent latrunculin A.

Main Results:

  • Actin is abundant both intranuclearly and in the cytoplasm of Amoeba proteus.
  • Intranuclear actin is predominantly G-actin, associated with chromatin, with minimal F-actin.
  • A distinct layer of unpolymerized actin is adjacent to the nuclear envelope, and a circumnuclear actin network surrounds the nucleus.

Conclusions:

  • The results indicate that G-actin plays a role in intranuclear organization and nuclear envelope structure in Amoeba proteus.
  • The circumnuclear actin system contributes to nuclear architecture but is distinct from intranuclear chromatin organization.
  • These findings support the conserved role of actin in fundamental nuclear processes, extending beyond multicellular organisms.