Polyubiquitin may stabilize tau filament structures in neurodegenerative diseases
In neurodegenerative diseases such as Alzheimer's disease, progressive neuronal damage is associated with the accumulation of abnormal tau filaments in the brain. The core of these filaments forms a highly ordered structure, while molecules such as ubiquitin are attached to tau around the core as post-translational modifications. However, the role these peripheral modifications play in…
Neurodegenerative diseases, including Alzheimer's disease, involve the buildup of abnormal tau filaments in the brain. These filaments have a highly structured core, with molecules like ubiquitin attaching to them as post-translational modifications. The impact of these peripheral modifications on tau filament stability is not fully understood.
In a study published in Nature Structural & Molecular Biology, researchers from the University of Tsukuba analyzed tau filaments from patients with Alzheimer's disease and vacuolar tauopathy, a rare inherited neurodegenerative disorder. Through experiments on mice and cryo-electron microscopy, the researchers discovered that filaments from the two diseases had distinct pathological patterns and varied filament types in vacuolar tauopathy.
By altering the position of polyubiquitin, the researchers observed changes in the interface between tau filaments' protofilaments, leading to novel filament structures. These findings suggest that the structure of tau filaments may be influenced not only by the core but also by surrounding post-translational modifications such as polyubiquitin.
This research provides valuable insights into the mechanisms behind the formation and stabilization of disease-specific tau filament structures, potentially deepening our understanding of the structural diversity seen in tau-related neurodegenerative diseases.
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