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Introduction to Actin

Introduction to Actin

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 different species.

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

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...

Actin Polymerization

Actin Polymerization

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 actin...

Actin Filament Depolymerization

Actin Filament Depolymerization

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...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

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 networks...

The Role of Actin and Myosin in Non-muscle Cells

The Role of Actin and Myosin in Non-muscle Cells

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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Updated: Jun 2, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Implications of oxidovanadium(IV) binding to actin.

Susana Ramos¹, Rui M Almeida, José J G Moura

¹REQUIMTE/CQFB, Departamento de Química, Faculdade de Ciências e Tecnologia, FCT, Universidade Nova de Lisboa, Caparica, Portugal. s.ramos@dq.fct.unl.pt

Journal of Inorganic Biochemistry

|April 19, 2011

Summary

Oxidovanadium(IV) binds to actin, causing conformational changes and inhibiting polymerization. This interaction highlights a potential mechanism for vanadium

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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

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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Actin is a crucial protein involved in muscle contraction and cell motility.
Vanadium compounds are known to exhibit various biological activities.
Understanding the interaction between metal ions and proteins is essential for elucidating cellular processes.

Purpose of the Study:

To investigate the binding interaction between oxidovanadium(IV) and actin.
To characterize the effects of oxidovanadium(IV) on actin structure and function.
To determine the impact of oxidovanadium(IV) on actin polymerization.

Main Methods:

Fluorescence spectroscopy was employed to study the binding of oxidovanadium(IV) to monomeric (G-actin) and polymerized (F-actin).
Stern-Volmer analysis was used to determine dissociation constants (K(d)).
Proton Nuclear Magnetic Resonance ((1)H NMR) spectroscopy was utilized to assess conformational changes in actin.
Inhibition of actin polymerization was measured in the presence of varying concentrations of oxidovanadium(IV).

Main Results:

Oxidovanadium(IV) effectively quenched the intrinsic fluorescence of both G-actin and F-actin, indicating binding.
High-affinity binding sites for oxidovanadium(IV) were identified on actin, with lower K(d) values for G-actin compared to F-actin.
Oxidovanadium(IV) induced local conformational changes in actin, particularly affecting the hydrophobic surface of G-actin.
(1)H NMR confirmed structural alterations in G-actin upon oxidovanadium(IV) treatment.
Oxidovanadium(IV) significantly inhibited G-actin polymerization in a dose-dependent manner, with complete suppression at 500 μM.

Conclusions:

Oxidovanadium(IV) binds to specific sites on actin, leading to conformational changes.
The binding of oxidovanadium(IV) interferes with actin polymerization.
These findings suggest a molecular mechanism for the cellular effects of vanadium compounds, potentially mediated through actin modulation.