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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...

The Role of Actin and Myosin in Non-muscle Cells

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They are held...

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...

Actin Filament Depolymerization

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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...

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...

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 different species.

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Related Experiment Video

Updated: Jun 9, 2026

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

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

Published on: May 5, 2022

Transiently crosslinked F-actin bundles.

Dan Strehle¹, Jörg Schnauss, Claus Heussinger

¹Soft matter physics division, Institute for Experimental Physics I, University of Leipzig, 04103, Leipzig, Germany. dan.strehle@uni-leipzig.de

European Biophysics Journal : EBJ

|August 25, 2010

Summary

F-actin bundles show distinct mechanical behaviors. They are elastic at short times but become elasto-plastic over longer durations, revealing complex cytoskeletal dynamics.

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Area of Science:

Cytoskeletal dynamics and biophysics.
Mechanics of biological polymers.

Background:

F-actin bundles are crucial eukaryotic cytoskeletal structures providing mechanical stability.
These bundles are stabilized by crosslinking proteins with rapid dissociation rates (around 1s⁻¹).
Despite rapid crosslinker turnover, actin bundles maintain long-term structural integrity.

Discussion:

Investigated mechanical response of reconstituted F-actin bundles using optical tweezers.
Observed differential mechanical behavior based on timescale of applied deformation.
Characterized relaxation times, revealing a broad distribution.

Key Insights:

F-actin bundles exhibit reversible elastic response at short timescales.
At longer timescales, bundles display irreversible elasto-plastic response, exceeding crosslinker dissociation rates.
Bundle relaxation is influenced by filament number, crosslinking details, and structural defects.

Outlook:

Further research into the precise mechanisms governing long-term actin bundle stability.
Exploring the role of crosslinker dynamics and filament organization in cellular mechanics.
Investigating how these mechanical properties contribute to cellular functions in vivo.