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Related Concept Videos

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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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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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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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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...
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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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Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

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Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
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Related Experiment Video

Updated: May 5, 2026

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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Relationships between fibronectin (LETS protein) and actin.

R O Hynes, A T Destree

    Cell
    |November 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Fibronectin and actin show coordinated distribution in spreading cells, suggesting a transmembrane link. This implies fibronectin

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

    • Cell biology
    • Biochemistry
    • Cytoskeleton research

    Background:

    • Fibronectin (LETS protein) is a key extracellular matrix protein.
    • Actin and intermediate filaments are major components of the cellular cytoskeleton.
    • Understanding the spatial relationship between these proteins is crucial for cell adhesion studies.

    Purpose of the Study:

    • To investigate the distribution of fibronectin, actin, and intermediate filaments in cultured cells.
    • To determine the relationship between fibronectin and cytoskeletal elements during cell spreading.
    • To explore fibronectin's potential role in cell attachment structures.

    Main Methods:

    • Double label immunofluorescence microscopy was employed.
    • Cultured cells were analyzed for the presence and distribution of fibronectin, actin, and intermediate filaments.

    Main Results:

    • No direct relationship was found between fibronectin and intermediate filaments.
    • Fibronectin and actin staining were coincident in many spreading cells.
    • Specific correlations were observed between actin and fibronectin patterns, especially in fibrillar arrays (80-100% correspondence).

    Conclusions:

    • Results suggest a transmembrane relationship between actin microfilament bundles and fibronectin.
    • Fibronectin may play a role in the formation of cell attachment plaques.
    • An interrelationship between attachment plaques, microfilaments, and fibronectin is proposed for cell-substratum and cell-cell contacts.