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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.

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...

Generation of Straight or Branched Actin Filaments

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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...

Fibrous Proteins

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

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Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

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Semiflexible filamentous composites.

E M Huisman¹, C Heussinger, C Storm

¹Universiteit Leiden, Instituut-Lorentz, Postbus 9506, NL-2300 RA Leiden, The Netherlands.

Physical Review Letters

|September 28, 2010

Summary

This summary is machine-generated.

This study models composite biopolymer networks. Stiff filaments protect floppy networks at low fractions, while high stiff filament fractions dominate mechanical response.

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Area of Science:

Biophysics
Materials Science
Polymer Physics

Background:

Biopolymer networks are ubiquitous in nature.
These networks often comprise both stiff and floppy filaments.
Understanding their mechanical properties is crucial.

Purpose of the Study:

Investigate mechanical behavior of composite biopolymer networks.
Explore stress and strain partitioning between stiff and floppy components.
Determine the relationship between network mechanics and filament fractions.

Main Methods:

Three-dimensional numerical simulations.
Modeling of interconnected stiff and floppy biopolymer filaments.
Analysis of microscopic stress and strain distribution.

Main Results:

Identified a nontrivial relationship between mechanical behavior and stiff polymer fraction.
Observed that low stiff filament fractions protect stiff inclusions within a floppy matrix.
Found that high stiff filament fractions lead to independent percolation and mechanical dominance by the stiff network.

Conclusions:

The mechanical response of composite biopolymer networks is highly dependent on the relative fraction of stiff filaments.
Network architecture significantly influences stress and strain partitioning.
These findings provide insights into natural and synthetic filamentous materials.