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Actin Polymerization and Cell Motility

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.

Introduction to Actin

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.

Generation of Straight or Branched Actin Filaments

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...

Cytoskeletal Accessory Proteins

Cytoskeletal Accessory Proteins

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...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

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 networks...

Actin Polymerization

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...

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Related Experiment Video

Updated: May 30, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Actin: from structural plasticity to functional diversity.

Cora-Ann Schoenenberger¹, Hans Georg Mannherz, Brigitte M Jockusch

¹M. E. Mueller Institute for Structural Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.

European Journal of Cell Biology

|August 9, 2011

Summary

This summary is machine-generated.

This review explores actin

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Area of Science:

Cell Biology
Biochemistry

Background:

Actin is a crucial protein involved in various cellular processes.
Understanding actin's structure-function relationship is key to deciphering its roles.

Purpose of the Study:

To review the history, discovery, purification, and structure of actin.
To highlight the link between actin's structure and its diverse functions.
To discuss unconventional actin conformations and their potential roles.

Main Methods:

Literature review and synthesis of existing research on actin.
Analysis of actin structure-function relationships.
Exploration of emerging concepts like unconventional actin conformations.

Main Results:

Actin's structure is intimately linked to its multiple cellular functions.
Unconventional actin conformations may be important for supramolecular organization.
These conformations might explain poorly understood nuclear actin activities.

Conclusions:

Actin's versatility stems from its adaptable structure.
Further research is needed to validate the in vivo existence and roles of unconventional actin conformations.
Investigating these conformations could unlock new insights into nuclear actin functions.