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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...
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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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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...
2.8K
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...
28.2K
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...
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.8K
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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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Intermediate Filaments: Structure and Assembly.

Harald Herrmann1, Ueli Aebi2

  • 1Functional Architecture of the Cell (B065), German Cancer Research Center (DKFZ), D-69120 Heidelberg, Germany, and Institute of Neuropathology, University Hospital Erlangen, D-91054 Erlangen, Germany.

Cold Spring Harbor Perspectives in Biology
|November 3, 2016
PubMed
Summary
This summary is machine-generated.

Intermediate filament (IF) proteins form the animal cytoskeleton and diverse biomaterials. Understanding their structure and mutations is key to deciphering IF diseases.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Intermediate filament (IF) proteins are essential structural components of the cytoskeleton in animal tissues.
  • These proteins feature an α-helical conformation, forming two-stranded coiled coils that build flexible, stress-resistant filaments.
  • IF proteins are highly charged, acting as versatile polyampholytes with diverse cellular functions.

Purpose of the Study:

  • To provide an overview of the molecular and structural parameters of IF proteins, using vimentin, keratins, and nuclear lamins as examples.
  • To highlight the capacity of IF proteins to assemble into diverse supramolecular structures and biomaterials.
  • To lay the groundwork for understanding how mutations in IF genes impact cellular functions and lead to IF diseases.

Main Methods:

  • Review of molecular and structural properties of IF proteins.
  • Analysis of supramolecular assembly capabilities.
  • Examination of the link between IF protein structure, function, and disease.

Main Results:

  • IF proteins exhibit specific α-helical structures enabling coiled-coil formation, the basis of cytoskeletal filaments.
  • These proteins assemble into a wide array of supramolecular structures, including cytoplasmic filaments, nuclear lamina, and extracellular appendages like hair and nails.
  • The structural versatility of IF proteins underlies their diverse functions and susceptibility to disease-causing mutations.

Conclusions:

  • IF proteins are fundamental to cellular structure and biomaterial formation across various locations in vertebrate organisms.
  • A detailed understanding of IF protein structure-function relationships is crucial for elucidating the pathogenesis of IF-related diseases.
  • Further research into IF protein mutations will enable a more rational approach to understanding and potentially treating IF diseases.