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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...

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...

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.

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...

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...

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...

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Related Experiment Video

Updated: Jun 24, 2026

Microfluidic Fabrication of Polymeric and Biohybrid Fibers with Predesigned Size and Shape

Microfluidic Fabrication of Polymeric and Biohybrid Fibers with Predesigned Size and Shape

Published on: January 8, 2014

In-fiber semiconductor filament arrays.

D S Deng¹, N D Orf, A F Abouraddy

¹Research Laboratory of Electronics, Department of Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.

|April 16, 2009

Summary

This summary is machine-generated.

A novel physical phenomenon transforms thin cylindrical shells into ordered filament arrays. This process, unlike droplet breakup, forms uniform axial structures, enabling nanometer-scale device fabrication.

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Using Vertically Aligned Carbon Nanofiber Arrays on Rigid or Flexible Substrates for Delivery of Biomolecules and Dyes to Plants

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Prescribed 3-D Direct Writing of Suspended Micron/Sub-micron Scale Fiber Structures via a Robotic Dispensing System

Prescribed 3-D Direct Writing of Suspended Micron/Sub-micron Scale Fiber Structures via a Robotic Dispensing System

Published on: June 12, 2015

Area of Science:

Physics
Materials Science
Nanotechnology

Background:

Classical fluid dynamics describe cylinder breakup into droplets via capillary instability.
Scaling processes in thin shells can lead to complex structural transformations.
Controlling nanoscale morphology is crucial for advanced electronic devices.

Purpose of the Study:

To investigate the physical phenomenon of cylindrical shell scaling.
To understand the mechanism behind the evolution into filament arrays.
To explore the fabrication of nanoscale devices using this phenomenon.

Main Methods:

Observation of a cylindrical shell undergoing a scaling process.
Analysis of the relationship between material viscosity and breakup tendency.
Utilizing a thermal drawing process to capture the filament array in a solid state.

Main Results:

A novel physical phenomenon where cylindrical shells form ordered filament arrays at a characteristic thickness.
Breakup tendency correlates with material viscosity, similar to capillary instability but in the cross-sectional plane.
Successful fabrication of solid sub-100 nm semiconductor filaments encapsulated in a polymer fiber.

Conclusions:

A fluid front instability mechanism is proposed for the observed cross-sectional structural evolution.
The thermal drawing process enables the creation of long, precisely oriented nanoscale filament arrays.
This method provides a pathway for fabricating nanodevices with simplified connectivity and unprecedented lengths.