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Related Concept Videos

The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

5.1K
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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Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

3.6K
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...
3.6K
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...
2.4K
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

4.4K
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...
4.4K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

25.8K
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...
25.8K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.3K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
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Related Experiment Video

Updated: Nov 30, 2025

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

Published on: March 6, 2018

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Recent insight into intermediate filament structure.

Sherif A Eldirany1, Ivan B Lomakin1, Minh Ho1

  • 1Department of Dermatology, Yale University, New Haven, CT, 06520, USA.

Current Opinion in Cell Biology
|November 15, 2020
PubMed
Summary
This summary is machine-generated.

Intermediate filaments (IFs) are crucial for cell function. Recent structural studies reveal new assembly mechanisms and binding interactions, advancing understanding of IF-related human diseases.

Keywords:
AssemblyBindingCrystallographyIntermediate filamentKeratinLaminStructureVimentin

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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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Three-dimensional Super Resolution Microscopy of F-actin Filaments by Interferometric PhotoActivated Localization Microscopy iPALM
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Intermediate filaments (IFs) are essential cytoskeletal components involved in numerous cellular processes across human tissues.
  • Understanding IF protein structure is critical for elucidating filament assembly, interactions with binding partners, and the development of targeted pharmacological agents.

Purpose of the Study:

  • To summarize recent advances in understanding the structure of intermediate filament proteins.
  • To connect these structural insights to IF assembly mechanisms, binding interactions, and human diseases.

Main Methods:

  • Review of recent structural studies on keratins, glial fibrillary acidic protein, and lamin.
  • Analysis of protein domains, including coiled-coil central-rod, N-terminal head, and C-terminal tail domains.
  • Examination of structural features such as knob-pocket tetramer formation, coil 1B inserts, helical linkers, and coil 2B residues.

Main Results:

  • Discoveries include a knob-pocket tetramer assembly in coil 1B, a lamin-specific coil 1B insert, flexible helical linkers in the rod domain, and key residues for filament assembly in coil 2B.
  • Identification of low-complexity, aromatic-rich kinked segments in head and tail domains of some IFs.
  • Structural data reveal that electrostatic surfaces are significant in the formation of IF complexes with binding partners.

Conclusions:

  • New structural data provide a deeper connection between intermediate filament protein structure, disease-causing mutations, and human clinical conditions.
  • These findings enhance the understanding of fundamental IF biology and their role in health and disease.