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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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Detergent Purification of Membrane Proteins01:18

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Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
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Actin Treadmilling01:18

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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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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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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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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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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Purification from starfish eggs of a protein that depolymerizes actin.

I Mabuchi

    Journal of Biochemistry
    |April 1, 1981
    PubMed
    Summary

    Researchers purified a protein from starfish eggs that rapidly depolymerizes filamentous actin (F-actin). This 17,000 molecular weight protein interacts with actin at a 1:1 ratio, similar to mammalian profilin.

    Area of Science:

    • * Biochemistry
    • * Cell Biology
    • * Molecular Biology

    Background:

    • * Actin polymerization is crucial for cellular processes.
    • * Proteins that regulate actin dynamics are essential for cell function.
    • * Understanding actin-binding proteins aids in deciphering cytoskeletal control.

    Purpose of the Study:

    • * To isolate and characterize a novel F-actin depolymerizing protein from starfish eggs.
    • * To determine the molecular weight and stoichiometry of interaction with actin.
    • * To compare the properties of this protein with known actin-binding proteins like profilin.

    Main Methods:

    • * Purification of the protein using DEAE-cellulose and hydroxylapatite column chromatography.
    • * Determination of apparent molecular weight.

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    Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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    Measuring Protein Binding to F-actin by Co-sedimentation
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    Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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  • * Analysis of actin polymerization inhibition and F-actin depolymerization.
  • * Molar ratio determination of protein-actin interaction.

    • Main Results:

    • * Successfully purified an F-actin depolymerizing protein from unfertilized starfish eggs.
    • * The purified protein has an apparent molecular weight of 17,000.
    • * The protein rapidly depolymerizes F-actin and inhibits actin polymerization.
    • * The protein interacts with actin at a 1:1 molar ratio.

    Conclusions:

    • * A novel actin depolymerizing protein was identified in starfish eggs.
    • * This protein shares functional similarities with mammalian profilin.
    • * The findings contribute to the understanding of actin regulation in non-mammalian species.