Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Introduction to Actin01:26

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.
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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.
Generation of Straight or Branched Actin Filaments01:14

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...
The Role of Actin and Myosin in Non-muscle Cells01:10

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...
Actin Polymerization01:42

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 Depolymerization01:19

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Iomeprol X-ray contrast media alter conformation and affinity of the ATP binding pocket of actin.

Biophysical journal·2026
Same author

Quantification of the Actin-Binding Protein Flightless-I in Human Serum by Automated Western Blot System and Investigation of Its Diagnostic Potential in Sepsis.

Biomedicines·2025
Same author

Efficient purification of soluble receptor for advanced glycation end-products from Sus scrofa lung tissue and synthesis of its binding ligand, glycated bovine serum albumin.

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences·2024
Same author

Cooperation of Various Cytoskeletal Components Orchestrates Intercellular Spread of Mitochondria between B-Lymphoma Cells through Tunnelling Nanotubes.

Cells·2024
Same author

Peripheral thickening of the sarcomeres and pointed end elongation of the thin filaments are both promoted by SALS and its formin interaction partners.

PLoS genetics·2024
Same author

Molecular Relay Stations in Membrane Nanotubes: IRSp53 Involved in Actin-Based Force Generation.

International journal of molecular sciences·2023

Related Experiment Video

Updated: Jun 10, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Conformational dynamics of actin: effectors and implications for biological function.

Gábor Hild1, Beáta Bugyi, Miklós Nyitrai

  • 1Department of Biophysics, University of Pécs, Faculty of Medicine, Pécs, Szigeti str. 12, H-7624, Hungary.

Cytoskeleton (Hoboken, N.J.)
|July 31, 2010
PubMed
Summary

Actin is a protein found in many cells, and it plays a variety of roles. This review looks at how actin's shape changes and how these changes affect its function. Actin interacts with other proteins, which may influence its structure. The review suggests that actin's ability to change shape is important for its versatility in the cell. Researchers examined existing studies to understand how actin's conformational changes support its biological roles. They found that actin-binding proteins may help modulate actin's shape. The review does not introduce new data but compiles current evidence. The findings suggest that actin's conformational dynamics are linked to its function, and further research is needed to clarify these mechanisms.

Keywords:
Actin conformational dynamicsActin-binding proteinsProtein structureCellular function

Frequently Asked Questions

More Related Videos

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

Published on: July 11, 2025

Related Experiment Videos

Last Updated: Jun 10, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

Published on: July 11, 2025

Area of Science:

  • Cell biology
  • Protein dynamics
  • Molecular biology

Background:

Actin is a protein found in many cell types. It has been shown to perform multiple roles in cellular processes. Over time, researchers have identified various actin structures and their functions. Actin-binding proteins contribute to the adaptability of actin. These proteins help shape actin's diverse morphology. However, the mechanisms behind actin's conformational changes remain unclear. This uncertainty has driven further investigation into actin's behavior. Understanding these dynamics could clarify actin's role in cellular function.

Purpose Of The Study:

This review aims to examine how actin's conformational states influence its biological roles. The study focuses on actin's interactions with binding proteins. Researchers want to clarify the relationship between actin's shape and its function. They also seek to summarize current findings on actin's adaptability. The goal is to highlight how actin's structure supports cellular versatility. The authors propose that actin's conformational changes are linked to function. This review does not introduce new data but compiles existing evidence. It provides a framework for understanding actin's dynamic behavior.

Main Methods:

The authors used a literature-based approach to analyze actin's conformational dynamics. They reviewed studies on actin-binding proteins and their interactions. The focus was on how these proteins influence actin's shape and function. Researchers examined prior findings on actin's structural transitions. They synthesized data from various experimental methods. The review included computational models and biochemical assays. The approach did not involve new experiments but compiled existing evidence. The goal was to identify patterns in actin's conformational behavior.

Main Results:

Actin's conformational states are closely linked to its function. The review found that actin's shape changes in response to binding proteins. These changes affect how actin interacts with other cellular components. The study highlights the role of actin-binding proteins in modulating function. Actin's flexibility allows it to adapt to different cellular needs. Researchers observed that actin's structure influences its ability to polymerize. The review also notes that actin's conformational transitions are essential for its activity. These findings suggest that actin's shape is a key factor in its biological roles.

Conclusions:

The authors suggest that actin's conformational dynamics are crucial for its biological roles. They propose that actin's shape changes in response to binding proteins. These changes may influence actin's interactions with other cellular components. The review highlights the importance of actin-binding proteins in modulating function. The findings suggest that actin's structure supports its versatility in cells. The authors do not claim that actin's conformational changes are the only factor in function. They propose that further research is needed to clarify these mechanisms. The review provides a foundation for future studies on actin's behavior.

The authors propose that actin's conformational states influence its interactions with binding proteins, which modulate its function.

Actin-binding proteins may induce structural changes in actin, allowing it to adapt to different cellular roles.

Actin's flexibility allows it to adopt different shapes, which may be necessary for its diverse roles in the cell.

Computational models help researchers simulate and predict actin's structural transitions under various conditions.

Biochemical assays and structural analyses have been used to measure actin's shape changes and interactions with binding proteins.

The authors suggest that actin's conformational changes may be essential for its function, but further research is needed to confirm this.