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Related Concept Videos

Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

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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...
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The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

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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...
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Assembly of Cytoskeletal Filaments01:18

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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...
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Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

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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...
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Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

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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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Types of Intermediate Filaments01:31

Types of Intermediate Filaments

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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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Lateral Subunit Coupling Determines Intermediate Filament Mechanics.

Charlotta Lorenz1, Johanna Forsting1, Anna V Schepers1

  • 1Institute for X-Ray Physics, University of Göttingen, Friedrich-Hund-Platz 1, 37077 Göttingen, Germany.

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|November 26, 2019
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Summary
This summary is machine-generated.

Researchers compared the mechanical properties of keratin and vimentin intermediate filaments (IFs). Vimentin

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Area of Science:

  • Biophysics
  • Cell Biology
  • Materials Science

Background:

  • The cytoskeleton provides mechanical support to cells.
  • Intermediate filaments (IFs) are key cytoskeletal components known for their extensibility.
  • Keratin and vimentin are crucial IFs with similar structures but distinct mechanical properties.

Purpose of the Study:

  • To compare the mechanical response of single keratin and vimentin filaments.
  • To elucidate the underlying molecular mechanisms governing their differential mechanical behaviors.

Main Methods:

  • Utilized optical tweezers to probe the mechanics of individual keratin and vimentin filaments.
  • Employed a computational model to analyze subunit interactions and unfolding dynamics.

Main Results:

  • Vimentin's mechanical properties are significantly influenced by buffer ionic strength.
  • Vimentin exhibits a high degree of subunit cooperativity, unlike keratin.
  • Computational modeling revealed strong lateral coupling of charged monomers in vimentin during alpha-helix unfolding.

Conclusions:

  • Cells can modulate their mechanical properties through the differential expression of keratin and vimentin.
  • Understanding these differences provides insights into cellular mechanics and adaptation.