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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

5.1K
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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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
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...
3.0K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.2K
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....
5.2K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
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...
2.9K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.1K
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...
3.1K
Actin Polymerization01:42

Actin Polymerization

6.5K
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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Related Experiment Video

Updated: Jun 25, 2025

Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Structural and functional mechanisms of actin isoforms.

Sarah M Heissler1, Krishna Chinthalapudi1

  • 1Department of Physiology and Cell Biology, Dorothy M. Davis Heart & Lung Research Institute, The Ohio State University, Columbus, OH, USA.

The FEBS Journal
|May 23, 2024
PubMed
Summary

Actin isoforms are crucial eukaryotic proteins with distinct roles. This review explores how their structure, modifications, and mutations impact cellular functions and disease.

Keywords:
actinactin isoformsactin‐binding proteinscontractilitycytoskeletonenzymologymechanobiologymutationsmyosinpost‐translational modifications

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • Actin is a fundamental eukaryotic protein essential for diverse cellular functions.
  • Cells maintain specific ratios of actin isoforms, primarily muscle and non-muscle actin.
  • Actin isoforms exhibit unique biochemistries, localizations, and interactions, influencing cytoskeletal dynamics.

Purpose of the Study:

  • To review the structural basis of actin isoform function.
  • To emphasize the impact of post-translational modifications and mutations on actin biochemistry and interactions.
  • To elucidate the role of actin isoforms in cellular regulation and disease.

Main Methods:

  • Literature review focusing on structural and functional studies of actin isoforms.
  • Analysis of research on post-translational modifications and disease-linked mutations affecting actin.
  • Examination of actin interactions with myosin motors and actin-binding proteins.

Main Results:

  • Actin isoform structure dictates specific biochemical properties and cellular roles.
  • Post-translational modifications and mutations significantly alter actin function and interactions.
  • Understanding these alterations is key to comprehending cytoskeletal regulation and associated diseases.

Conclusions:

  • The structure of actin isoforms is intrinsically linked to their diverse cellular functions.
  • Investigating modifications and mutations provides critical insights into actin-related cellular processes and pathologies.
  • This knowledge is vital for understanding health and disease at a molecular level.