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Related Concept Videos

Disassembly of Intermediate Filaments01:35

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...
Formation of Intermediate Filaments00:57

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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 Filaments01:19

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...
Types of Intermediate Filaments01:31

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...
Assembly of Cytoskeletal Filaments01:18

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...
Adaptability of Cytoskeletal Filaments01:12

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The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...

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Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
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Self-consistent field theory for the interactions between keratin intermediate filaments.

Anna Akinshina1, Etienne Jambon-Puillet, Patrick B Warren

  • 1Unilever R&D Port Sunlight, Quarry Road East, Bebington, Wirral, CH63 3JW, UK. anna.akinshina@manchester.ac.uk.

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|September 7, 2013
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Summary

Keratin filaments interact through their disordered domains, influencing skin elasticity. This interaction is sensitive to charge balance and the surrounding medium, explaining tissue flexibility.

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Area of Science:

  • Biophysics
  • Materials Science

Background:

  • Keratins are crucial structural proteins in skin, hair, and nails.
  • Keratin Intermediate Filaments (KIFs) form the bulk of corneocytes in the Stratum Corneum.
  • KIF interactions are hypothesized to govern skin elasticity.

Purpose of the Study:

  • To model the interactions between keratin intermediate filaments.
  • To understand the role of disordered keratin domains in filament interactions and skin elasticity.

Main Methods:

  • Developed a self-consistent field theory model for KIF interactions.
  • Represented KIFs as charged surfaces with grafted charged heteropolymers (disordered domains).
  • Utilized an amino acid resolution protein model for terminal domains.

Main Results:

  • Identified a weak attraction between keratin surfaces mediated by terminal chains.
  • Attribution of attraction to bridging and electrostatic forces near charge compensation.
  • Observed disappearance of attraction with deviations from charge compensation or addition of ions/amino acids.

Conclusions:

  • Physico-chemical properties of disordered domains and medium composition control KIF interactions.
  • Findings align with experimental observations on keratin-containing tissues.
  • Supports the model that KIF interactions contribute to tissue elastic properties.