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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

6.9K
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 Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

7.1K
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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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.8K
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...
3.8K
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

4.2K
The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
4.2K
Actin Polymerization01:42

Actin Polymerization

8.9K
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...
8.9K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

4.1K
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...
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Related Experiment Video

Updated: Mar 24, 2026

Measuring Protein Binding to F-actin by Co-sedimentation
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Measuring Protein Binding to F-actin by Co-sedimentation

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Actin and Actin-Binding Proteins.

Thomas D Pollard1

  • 1Departments of Molecular, Cellular, and Developmental Biology, of Molecular Biophysics and Biochemistry, and of Cell Biology, Yale University, New Haven, Connecticut 06520-8103.

Cold Spring Harbor Perspectives in Biology
|March 19, 2016
PubMed
Summary
This summary is machine-generated.

Actin filaments are essential for cell structure and movement in all organisms. Numerous proteins regulate actin

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Related Experiment Videos

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

  • Cell Biology
  • Biochemistry

Background:

  • Actin filaments are crucial for cellular structure, motility, and internal transport in eukaryotes.
  • Myosin motor proteins generate force on actin filaments through adenosine triphosphate (ATP) hydrolysis.

Purpose of the Study:

  • To provide a comprehensive overview of actin properties.
  • To detail the roles of accessory proteins in regulating actin filament dynamics.

Main Methods:

  • Literature review of actin polymerization and regulation.
  • Analysis of protein interactions controlling actin assembly and disassembly.

Main Results:

  • Actin polymerization is a spontaneous process followed by ATP hydrolysis.
  • Dozens of proteins modulate actin dynamics by controlling nucleotide exchange, polymerization initiation, and filament capping.
  • Proteins also regulate phosphate dissociation, filament cross-linking, and severing.

Conclusions:

  • Actin's dynamic assembly and disassembly are tightly controlled by a complex network of regulatory proteins.
  • Understanding these regulatory mechanisms is key to comprehending fundamental cellular processes.