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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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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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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 Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

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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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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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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Disease-specific tau filaments assemble via polymorphic intermediates.

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  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

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Researchers uncovered the initial intermediate amyloid filament structure in tau protein assembly, crucial for understanding neurodegenerative diseases like Alzheimer's and informing new therapeutic strategies.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Intermediate species in amyloid filament assembly are implicated in neurodegenerative diseases.
  • Structural data on these intermediates is limited, hindering understanding of amyloid assembly mechanisms.

Purpose of the Study:

  • To investigate the in vitro assembly of truncated tau protein into amyloid filaments.
  • To determine the structural characteristics of intermediate species during filament formation.

Main Methods:

  • Time-resolved cryogenic electron microscopy (cryo-EM) was employed to study tau assembly.
  • Nuclear magnetic resonance (NMR) was used to analyze monomeric tau conformations.

Main Results:

  • A shared initial intermediate amyloid filament was identified, featuring an ordered core (residues 302-316).
  • This core structure was also observed in monomeric tau, adopting rigid, beta-strand-like conformations.
  • Subsequent time points revealed diverse intermediate structures dependent on reaction conditions, with most disappearing by the end of the reaction.
  • Final filaments retained ordered cores consistent with those found in human brain samples.

Conclusions:

  • The study provides structural insights into primary and secondary nucleation in amyloid assembly.
  • Findings offer potential targets for developing novel therapeutics for neurodegenerative diseases.