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Related Concept Videos

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 Polymerization01:42

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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

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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.
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Actin Filament Depolymerization01:19

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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).
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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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Assembly of Cytoskeletal Filaments01:18

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Fullerenol Nanoparticles with Structural Activity Induce Variable Intracellular Actin Filament Morphologies.

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    Fullerenol nanoparticles interact with actin, altering its structure and potentially inhibiting cell movement. One fraction binds strongly, forming rods and possibly causing side effects.

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    Area of Science:

    • Nanotechnology
    • Biochemistry
    • Cell Biology

    Background:

    • Fullerenol nanoparticles show diverse biological effects.
    • Actin is a dynamic structural protein crucial for cell function.
    • Different fullerenol fractions possess varied surface chemistries.

    Purpose of the Study:

    • To investigate the interaction between two fullerenol fractions and actin.
    • To determine how fullerenol binding affects actin filament morphology.
    • To elucidate the molecular mechanisms underlying fullerenol-actin interactions.

    Main Methods:

    • Separation and purification of fullerenol fractions.
    • Molecular simulations to analyze binding interactions.
    • Assessment of changes in actin filament structure and cell effects.

    Main Results:

    • One fullerenol fraction with specific surface charges (-1.913 ± 0.008q x10^-6 C) and C-OH/C=O percentages (16.14 ± 0.60% and 17.55 ± 0.69%) strongly binds to actin via hydrogen bonds.
    • Molecular simulations confirmed specific binding sites and modes between this active fullerenol and actin.
    • Binding induced actin morphological changes, potentially transforming ATP-actin to ADP-actin, facilitating cofilin binding and filament severing, forming cofilin/actin/fullerenol rods.

    Conclusions:

    • Fullerenol nanoparticles can bind to actin and disrupt its filament structure.
    • The specific surface chemistry of fullerenols dictates their interaction with actin.
    • Disruption of actin dynamics by fullerenols may inhibit cell locomotion or lead to chronic side effects.