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Related Concept Videos

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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Introduction to Actin01:26

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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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Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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Actin Polymerization and Cell Motility01:13

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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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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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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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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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Updated: Jun 11, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Differential interference with actin-binding protein function by acute Cytochalasin B.

Christopher Lambert, Marius Karger, Anika Steffen

    Biorxiv : the Preprint Server for Biology
    |October 7, 2024
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    This summary is machine-generated.

    Cytochalasin B and D unexpectedly enhance the accumulation of actin barbed end-binding proteins, like Ena/VASP and capping protein, in cell lamellipodia, revealing new effects on dynamic actin structures.

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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
    • Molecular Biology

    Background:

    • Dynamic actin filament remodeling is essential for critical cellular processes.
    • Cytochalasins B and D are fungal metabolites used to study actin dynamics.
    • The precise molecular mechanisms of cytochalasin action on dynamic actin structures remain unclear.

    Purpose of the Study:

    • To investigate the molecular effects of cytochalasin B on actin barbed end-binding proteins in live migrating cells.
    • To elucidate the specific interactions and dynamics of these proteins upon cytochalasin treatment.

    Main Methods:

    • Live cell imaging of fluorescently labeled actin-binding proteins.
    • Acute treatment of migrating cell lamellipodia with cytochalasin B.
    • Analysis of protein dynamics and accumulation at barbed ends.

    Main Results:

    • Cytochalasin B treatment halted lamellipodium protrusion but increased accumulation of Ena/VASP and capping protein (CP) at barbed ends.
    • These effects were specific, with VASP accumulation dependent on CP.
    • Cytochalasin B also enhanced apparent CP barbed end interactions and mimicked Arp2/3 complex activity.

    Conclusions:

    • Cytochalasins exert novel effects on barbed end-binding factors beyond simple polymerization inhibition.
    • These findings necessitate a re-evaluation of how cytochalasins impact dynamic actin structures.
    • The study reveals a new spectrum of cytochalasin activities with implications for cell migration and development research.