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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.

The Structure of Intermediate Filaments

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm). These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...

Disassembly of Intermediate Filaments

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

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...

Types of Intermediate Filaments

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...

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...

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Related Experiment Video

Updated: Jun 24, 2026

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: July 20, 2022

An in vivo intermediate filament assembly model.

Stéphanie Portet¹, Julien Arino

¹Department of Mathematics, University of Manitoba, Winnipeg, MB, Canada. portets@cc.umanitoba.ca

Mathematical Biosciences and Engineering : MBE

|March 19, 2009

Summary

This study models intermediate filament organization, revealing that posttranslational modifications controlling protein solubility are key regulators. Increased solubilization promotes filament aggregation into particles.

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Area of Science:

Cellular Biology
Biophysics
Systems Biology

Background:

Intermediate filaments (IFs) are crucial cytoskeletal components.
Their organization into soluble proteins, particles, and filaments is dynamic and complex.
Understanding IF organization is vital for cellular structure and function.

Purpose of the Study:

To develop a mathematical model for in vivo intermediate filament organization.
To analyze the equilibrium and stability of the IF system.
To identify key regulatory factors influencing IF structural states.

Main Methods:

Development of a mathematical model for IF organization.
Analysis of system equilibrium and stability.
Sensitivity analysis to determine parameter influence.

Main Results:

The model demonstrates a unique, globally stable equilibrium for IF organization.
Posttranslational modifications (PTMs) significantly influence IF organization.
Increased PTM-induced solubilization favors aggregation into particles.

Conclusions:

PTMs regulating intermediate filament protein solubility are primary controllers of IF organization.
Signaling pathways that enhance filament solubilization can lead to particle formation.
The model provides insights into the dynamic regulation of the cytoskeleton.