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Related Concept Videos

The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

6.0K
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...
6.0K
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

4.1K
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...
4.1K
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

5.1K
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...
5.1K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.8K
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...
2.8K
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

10.5K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
10.5K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.3K
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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Related Experiment Video

Updated: Mar 26, 2026

Imaging Intermediate Filaments and Microtubules with 2-dimensional Direct Stochastic Optical Reconstruction Microscopy
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Imaging Intermediate Filaments and Microtubules with 2-dimensional Direct Stochastic Optical Reconstruction Microscopy

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How to Study Intermediate Filaments in Atomic Detail.

Anastasia A Chernyatina1, John F Hess2, Dmytro Guzenko1

  • 1Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Leuven, Belgium.

Methods in Enzymology
|January 23, 2016
PubMed
Summary

Understanding intermediate filament (IF) structure requires atomic detail. This review covers bioinformatics, X-ray crystallography, and EPR methods crucial for elucidating IF dimer structure and disease mutations.

Keywords:
Amino-acid sequence analysisCoiled coilCrystallizationElectron paramagnetic resonanceFilament assemblySite-directed spin labelingThree-dimensional structureX-ray crystallography

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Three-dimensional Super Resolution Microscopy of F-actin Filaments by Interferometric PhotoActivated Localization Microscopy iPALM
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Three-dimensional Super Resolution Microscopy of F-actin Filaments by Interferometric PhotoActivated Localization Microscopy iPALM
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Intermediate filaments (IFs) are essential cytoskeletal proteins.
  • Understanding IF structure is key to their function and disease mechanisms.
  • The coiled-coil dimer is the fundamental building block of IFs.

Purpose of the Study:

  • To review methods for determining IF dimer structure.
  • To highlight advances in understanding IF structure-function relationships.
  • To discuss structural insights into disease-related IF mutations.

Main Methods:

  • Bioinformatics analysis for insights into dimer structure, including poorly accessible regions.
  • X-ray crystallography of IF protein fragments to atomic resolution using a "divide-and-conquer" approach.
  • Electron paramagnetic resonance (EPR) with site-directed spin labeling to probe proximity and mobility within IFs.

Main Results:

  • Atomic resolution structures of IF dimer building blocks have been achieved.
  • Bioinformatics provides insights into regions difficult to study experimentally.
  • EPR reveals details of dimer structure and dimer-dimer contacts.

Conclusions:

  • A combination of bioinformatics, X-ray crystallography, and EPR has significantly advanced understanding of IF dimer structure.
  • These structural insights are vital for mechanistic understanding of IF-related diseases.
  • Optimized methods and awareness of limitations enhance the efficiency of structural studies.