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Related Concept Videos

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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The Structure of Intermediate Filaments01:19

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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.
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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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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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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.
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Assembly of Complex Microtubule Structures01:32

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Related Experiment Video

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Experimental Approaches for Biochemical Analysis of Glial Fibrillary Acidic Protein and Its Disease-associated Variants
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Explaining intermediate filament accumulation in giant axonal neuropathy.

Puneet Opal1, Robert D Goldman2

  • 1Department of Cell and Molecular Biology; Northwestern University Feinberg School of Medicine; Chicago, IL USA ; Davee Department of Neurology; Northwestern University Feinberg School of Medicine; Chicago, IL USA.

Rare Diseases (Austin, Tex.)
|July 9, 2014
PubMed
Summary

Giant axonal neuropathy (GAN) is caused by mutations affecting gigaxonin, a protein crucial for degrading intermediate filaments. This study reveals gigaxonin regulates intermediate filament degradation, explaining GAN

Keywords:
BTB/Kelchgiant axonal neuropathygigaxoninintermediate filamentsneurofilamentsvimentin

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Genetics

Background:

  • Giant axonal neuropathy (GAN) is a rare genetic disorder.
  • It results from mutations in the GAN gene, affecting gigaxonin protein.
  • GAN causes intermediate filament aggregation, particularly in neurons, leading to giant axons.

Purpose of the Study:

  • To elucidate the underlying mechanism of intermediate filament pathology in GAN.
  • To understand the normal function of gigaxonin in relation to intermediate filaments.

Main Methods:

  • Investigated the role of gigaxonin in regulating intermediate filament protein degradation.
  • Utilized proteasome-mediated degradation pathways as a focus.

Main Results:

  • Demonstrated that gigaxonin normally regulates the degradation of intermediate filament proteins.
  • Established the first direct link between GAN mutations and intermediate filament pathology.
  • Identified gigaxonin's role in proteasomal degradation of intermediate filaments.

Conclusions:

  • Gigaxonin's function is essential for preventing intermediate filament aggregation.
  • Understanding gigaxonin's role provides insight into GAN pathogenesis.
  • Findings have broader implications for diseases involving intermediate filament aggregation.