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Related Concept Videos

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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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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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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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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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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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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Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Related Experiment Video

Updated: Jan 21, 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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Completion of the Vimentin Rod Domain Structure Using Experimental Restraints: A New Tool for Exploring Intermediate

David D Gae1, Madhu S Budamagunta2, John F Hess3

  • 1Department of Surgery, School of Medicine, University of California San Francisco, San Francisco, CA 94118, USA.

Structure (London, England : 1993)
|August 13, 2019
PubMed
Summary

Researchers determined the complete structure of the intermediate filament rod domain using electron paramagnetic resonance (EPR) and molecular modeling. This provides the first experimentally driven model for vimentin, aiding further research.

Keywords:
EPRESRUCSF chimera: macromolecular structureelectron paramagnetic resonanceintermediate filamentsmolecular dynamicsmolecular modelingsite-directed spin labelingvimentin

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Intermediate filaments, like vimentin, are crucial cytoskeletal components.
  • Previous studies elucidated structures of vimentin's central rod domain using EPR and X-ray crystallography.

Purpose of the Study:

  • To determine the structure and dynamics of the uncharacterized linker 1-2 (L1-2) region of vimentin.
  • To integrate existing structural data into a complete model of the vimentin rod domain.

Main Methods:

  • Electron paramagnetic resonance (EPR) spectroscopy on full-length vimentin.
  • X-ray crystallography of vimentin peptides.
  • Molecular modeling and molecular dynamic (MD) simulations.

Main Results:

  • EPR and X-ray data showed high concordance for previously solved regions.
  • MD simulations of the constructed model aligned with EPR-determined spin label motion.
  • MD simulations revealed heterogeneity and concerted state switching within the L1-2 region.

Conclusions:

  • An experimentally validated, complete model of the intermediate filament rod domain was generated.
  • This model serves as a valuable tool for future vimentin assembly and modeling studies.
  • The study provides novel insights into the dynamics of the vimentin L1-2 region.