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Related Concept Videos

The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

4.0K
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

3.1K
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...
3.1K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

19.6K
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...
19.6K
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

3.7K
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...
3.7K
Fibrous Proteins00:55

Fibrous Proteins

2.1K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
2.1K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
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...
2.1K

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Vimentin filaments integrate low-complexity domains in a complex helical structure.

Matthias Eibauer1, Miriam S Weber2, Rafael Kronenberg-Tenga2

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Researchers revealed the 3D structure of vimentin intermediate filaments (IFs), uncovering a unique helical assembly. This finding explains the remarkable mechanical strength and stretchability of these crucial cytoskeletal biopolymers.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Structural Biology

Background:

  • Intermediate filaments (IFs) are essential cytoskeletal components.
  • They confer tissue-specific mechanical properties and participate in cellular processes.
  • The 3D structure of IFs has been difficult to determine due to their complex architecture.

Purpose of the Study:

  • To elucidate the three-dimensional structure of vimentin intermediate filaments (VIFs).
  • To understand the structural basis for the mechanical properties of VIFs.

Main Methods:

  • Cryo-focused ion-beam milling
  • Cryo-electron microscopy
  • Cryo-electron tomography

Main Results:

  • Vimentin IFs assemble into a modular, intertwined, flexible helical structure.
  • The cross-section reveals 40 α-helices organized into five protofibrils.
  • Intrinsically disordered head domains form an internal fiber, while disordered tails create lateral connections.

Conclusions:

  • The 3D structure of VIFs is a complex, modular helical assembly.
  • Disordered protein domains play a critical role in VIFs' mechanical strength and stretchability.
  • This study provides a structural basis for understanding IF biopolymer function.