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Related Concept Videos

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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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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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...
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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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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Introduction to Actin01:26

Introduction to Actin

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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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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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Related Experiment Video

Updated: May 2, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Actin cytoskeleton: a nucleator face-off.

James B Moseley1

  • 1Department of Biochemistry, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.

Current Biology : CB
|March 8, 2014
PubMed
Summary

Actin assembly proteins control cell structure by competing for actin monomers. This competition maintains a balance, or homeostasis, between the cell's various actin networks.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Biophysics

Background:

  • Actin assembly proteins are crucial for forming diverse cytoskeletal structures within a cell.
  • Understanding the regulation of actin dynamics is fundamental to cell biology.

Purpose of the Study:

  • To investigate the competitive interactions among actin assembly factors.
  • To elucidate the mechanism by which homeostasis is achieved in actin networks.

Main Methods:

  • The study likely involved in vitro biochemical assays to measure protein-protein and protein-actin interactions.
  • Advanced microscopy techniques may have been used to visualize actin network formation in real-time.

Main Results:

  • Assembly factors were found to directly compete for binding to actin monomers.

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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy
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  • This competition results in a homeostatic mechanism that balances the formation of different actin structures.
  • The findings reveal a novel regulatory principle governing cytoskeletal organization.

    • Conclusions:

    • Actin monomer availability is a key limiting factor regulated by competing assembly proteins.
    • This competitive binding mechanism ensures the stable and balanced construction of the actin cytoskeleton.
    • The study provides new insights into the fundamental processes of cellular structure formation and maintenance.