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Actin Filament Depolymerization

Actin Filament Depolymerization

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...

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...

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.

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...

Assembly of Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

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...

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.

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Related Experiment Video

Updated: May 30, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.

Bishal K Singh¹, Julia M Sattler, Moon Chatterjee

¹Department of Biochemistry, University of Oulu, PO Box 3000, 90014 Oulu, Finland.

The Journal of Biological Chemistry

|August 12, 2011

Summary

Plasmodium parasites use actin motors for invasion. This study reveals Plasmodium actin depolymerization factor 2 (ADF2) binds and severs actin filaments, unlike ADF1, aiding parasite motility.

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Last Updated: May 30, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Understanding the Development of Compensatory Pathways in a Mutant Malaria Parasite Harbouring Hypomorphic Allele of Plant-Like Kinases

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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

Area of Science:

Cell Biology
Parasitology
Biochemistry

Background:

Apicomplexan parasites, including Plasmodium, rely on actin-based motility for host cell invasion.
Parasitic actin regulation involves unique, poorly conserved proteins, including actin depolymerization factors (ADFs).
Plasmodium possesses two ADFs (ADF1 and ADF2) with low sequence homology to each other and mammalian orthologs.

Purpose of the Study:

To characterize the biochemical and structural properties of Plasmodium ADF1 and ADF2.
To understand the distinct roles of these ADFs in regulating parasite actin dynamics.
To elucidate the structural basis for their functional differences.

Main Methods:

Biochemical assays to assess actin binding, filament severing, and nucleotide exchange.
Protein crystallization and X-ray crystallography to determine the structure of Plasmodium ADF1.
Sequence and structural comparisons between Plasmodium ADFs and known ADF/cofilin family members.

Main Results:

Plasmodium ADF2 exhibits canonical ADF activity, binding globular and filamentous actin, severing filaments, and promoting nucleotide exchange.
Plasmodium ADF1 displays significantly different structural features compared to the ADF consensus, explaining its lack of filamentous actin binding.
Plasmodium ADF2's structure closely resembles that of canonical ADF/cofilin proteins.

Conclusions:

Plasmodium ADF2 functions as a classical actin depolymerization factor, crucial for parasite actin dynamics.
The unique structure of Plasmodium ADF1 accounts for its divergent functional properties.
Understanding these parasite-specific actin regulators offers potential targets for antimalarial drug development.