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Related Concept Videos

Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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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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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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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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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Actin Treadmilling01:18

Actin Treadmilling

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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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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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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Actin dynamics in protein homeostasis.

Thomas D Williams1, Adrien Rousseau1

  • 1MRC-Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, U.K.

Bioscience Reports
|August 31, 2022
PubMed
Summary

This review explores how actin structures influence protein homeostasis. Actin is a key cytoskeletal component that forms structures sensitive to the cell environment. These structures interact with factors involved in mRNA and protein regulation. The review highlights how actin structures change under stress conditions, potentially affecting transcription and degradation processes. The findings suggest that actin plays a critical role in maintaining cellular balance. This role is observed across various eukaryotic organisms. The authors propose that actin is an important but often overlooked regulator of protein homeostasis.

Keywords:
ActinCell stressprotein homeostasisprotein regulationproteostasisactin cytoskeletonprotein regulationcellular homeostasismRNA transcription

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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Area of Science:

  • Cell biology
  • Protein homeostasis research
  • Cytoskeletal dynamics

Background:

Protein homeostasis is essential for maintaining cell function and adapting to environmental changes. Prior research has shown that cells adjust protein levels and structures in response to external and internal signals. However, the role of cytoskeletal components in this process remains unclear. No prior work had resolved how actin structures specifically contribute to protein regulation. This gap motivated a deeper investigation into actin’s involvement in protein homeostasis. Actin is known to form diverse structures that are sensitive to cellular conditions. These structures may interact with mRNA and protein regulation systems. Understanding these interactions could clarify how actin influences protein homeostasis.

Purpose Of The Study:

This review aims to explore the relationship between actin dynamics and protein homeostasis. The specific problem is understanding how actin structures influence mRNA and protein regulation. The motivation comes from the lack of clarity on actin’s role in this context. Actin is a major cytoskeletal component, yet its regulatory functions are often overlooked. The study focuses on how actin structures change under stress conditions. These changes may affect mRNA transcription and protein degradation processes. The goal is to synthesize current evidence on actin’s role in protein homeostasis. This synthesis could help clarify how actin contributes to maintaining cellular balance.

Main Methods:

The authors conducted a literature review to analyze existing findings on actin and protein homeostasis. They examined how actin structures interact with mRNA and protein regulation systems. The review approach included analyzing studies on actin’s sensitivity to environmental changes. They focused on how these structures influence transcription and degradation processes. The authors synthesized findings from multiple disciplines, including cell biology and biochemistry. They evaluated how actin structures respond to stress conditions. The approach involved comparing results from different experimental models. This method allowed the authors to highlight key findings from the literature.

Main Results:

Actin structures are acutely sensitive to the cell environment and may influence protein regulation. These structures interact with factors involved in mRNA and protein production. The review found that actin plays a critical role in regulating these processes. Actin structures may alter mRNA transcription under stress conditions. Protein degradation pathways may also be affected by changes in actin dynamics. The findings suggest that actin contributes to maintaining protein homeostasis. This role is observed across various eukaryotic organisms. The evidence supports actin as a key regulator of protein homeostasis.

Conclusions:

The authors propose that actin structures are important for protein homeostasis. These structures may influence mRNA and protein regulation systems. The synthesis of findings suggests actin’s role is often overlooked in this context. The review highlights how actin structures change under stress conditions. These changes may affect transcription and degradation processes. The authors suggest that actin contributes to maintaining cellular balance. This conclusion is based on evidence from multiple studies. The findings may help guide future research on actin’s regulatory functions.

Actin structures interact with mRNA and protein regulation systems, potentially altering transcription and degradation processes.

Actin structures are acutely sensitive to the cell environment and may change under stress conditions.

Actin is a major cytoskeletal component, but its regulatory functions are not always recognized in protein homeostasis research.

Actin structures may influence mRNA transcription by interacting with regulatory factors under stress conditions.

Changes in actin dynamics may impact protein degradation pathways, contributing to protein homeostasis.

The authors suggest that actin is an important but often overlooked regulator of protein homeostasis across eukaryotes.