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Formation of Intermediate Filaments

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.

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...

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...

Restarting Stalled Replication Forks

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...

Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

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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Updated: Jun 14, 2026

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

Published on: October 25, 2017

Confining potential when a biopolymer filament reptates.

Bo Wang¹, Juan Guan, Stephen M Anthony

¹Departments of Materials Science and Engineering, University of Illinois, Urbana, Illinois 61801 USA.

Physical Review Letters

|April 7, 2010

Summary

We tracked the movement of entangled actin filaments to understand their behavior in confined spaces. Our findings reveal distinct force regimes and model the filament tube width distribution.

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Area of Science:

Biophysics
Polymer Physics

Background:

Filamentous actin (F-actin) networks are crucial in cell mechanics.
Understanding F-actin behavior in confined environments is key to cell function.

Purpose of the Study:

To investigate the confining potential and Brownian motion of entangled F-actin filaments.
To characterize the mechanical response and heterogeneity of F-actin chains.

Main Methods:

Single-molecule fluorescence imaging was employed to track F-actin motion.
Analysis focused on Brownian motion perpendicular to the filament contour.

Main Results:

A Hookean regime at small displacements transitioned to a large-amplitude regime.
The effective restoring force became independent of displacement in the large-amplitude regime.
A model was developed for implied heterogeneity based on tube width distribution.

Conclusions:

Entangled F-actin exhibits complex mechanical responses under confinement.
The study provides a model for F-actin heterogeneity relevant to cellular environments.