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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

6.8K
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...
6.8K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

7.0K
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....
7.0K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.9K
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...
3.9K
Actin Polymerization01:42

Actin Polymerization

8.8K
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...
8.8K
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
Actin Treadmilling01:18

Actin Treadmilling

10.0K
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...
10.0K

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Physical Confinement Modulates the Rate-Limiting Transition in the Release of Phosphate from Actin Filaments.

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Guidelines for Successful Actin Polymerization Experiments.

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Addendum: CYTOPLASMIC FILAMENTS OF AMOEBA PROTEUS: I. The Role of Filaments in Consistency Changes and Movement.

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Reaching the full potential of cryo-EM reconstructions with molecular dynamics simulations at 310 K: Actin filaments as an example.

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Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.

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Related Experiment Video

Updated: Mar 11, 2026

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

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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What We Know and Do Not Know About Actin.

Thomas D Pollard1,2,3

  • 1Department of Molecular Cellular and Developmental Biology, Yale University, 208103, New Haven, CT, 06520-8103, USA. thomas.pollard@yale.edu.

Handbook of Experimental Pharmacology
|November 23, 2016
PubMed
Summary
This summary is machine-generated.

Actin research has advanced significantly, but key knowledge gaps remain, hindering our understanding of actin-dependent cellular processes. Future work must focus on mechanistic insights to fully elucidate actin biology.

Keywords:
ActinArp2/3 complexCapping proteinCofilinProfilin

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

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Related Experiment Videos

Last Updated: Mar 11, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Seven decades of research have elucidated actin structure, assembly, regulatory proteins, and cellular functions.
  • Despite extensive study, critical information gaps persist, impeding a comprehensive understanding of actin-dependent mechanisms.

Purpose of the Study:

  • To summarize current knowledge on actin biology.
  • To identify research gaps and propose future directions for mechanistic understanding.

Main Methods:

  • Literature review and synthesis of existing research on actin.
  • Identification of key areas requiring further investigation.

Main Results:

  • A comprehensive overview of the current state of actin research.
  • Examples of critical experiments needed to fill knowledge gaps.

Conclusions:

  • Significant progress has been made in understanding actin.
  • A mechanistic understanding of actin biology requires targeted future research efforts.