Related Experiment Video
Updated: Sep 10, 2025
09:22
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
18.5K
Interactions with tau's microtubule-binding repeats modulate amyloid-β aggregation and toxicity
Mingeun Kim1, Yuxi Lin2, Eunju Nam1
1Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Republic of Korea.
Nature Chemical Biology
|August 22, 2025
Summary
Researchers discovered how tau protein fragments interact with amyloid-beta (Aβ) to alter Aβ aggregation and toxicity in Alzheimer's disease (AD) pathogenesis. This tau-Aβ interplay offers new therapeutic targets for AD.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Alzheimer's disease (AD) pathogenesis involves tau neurofibrillary tangles and amyloid-beta (Aβ) plaques.
- The individual roles of tau and Aβ are studied, but their interaction in AD is not fully understood.
Purpose of the Study:
- To investigate the molecular mechanisms of tau and Aβ interaction.
- To understand how this interaction influences Aβ aggregation and toxicity.
Main Methods:
- Molecular-level mechanistic investigations.
- Analysis of tau's microtubule-binding domain fragments.
Main Results:
- Tau's microtubule-binding repeats engage with Aβ distinctly.
- This interaction modifies Aβ aggregation and toxicity in extracellular and intracellular environments.
- Specific tau fragments with balanced hydrophobic/hydrophilic properties promote hetero-adduct formation with Aβ.
Conclusions:
- The interplay between tau and Aβ is crucial in Alzheimer's disease pathogenesis.
- Targeting the tau-Aβ interaction presents a potential therapeutic strategy for AD.
Related Concept Videos
03:03Amyloid Fibrils
9.9K
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,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.9K
01:42Microtubule Associated Proteins (MAPs)
4.5K
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
4.5K
01:15Drugs that Stabilize Microtubules
2.1K
Microtubules are dynamic structures that undergo cycles of catastrophe and rescue. The microtubules play a central role in cell division by forming the spindle apparatus for segregating the chromosomes. This makes them ideal targets for regulating dividing cells in tumors and malignant cancer cells. Microtubule stabilizing drugs help stabilize the microtubule formation and promote its polymerization. Paclitaxel was the first microtubule stabilizing agent used as anticancer drug in chemotherapy...
2.1K