Polyubiquitin may stabilize tau filament structures in neurodegenerative diseases

by University of Tsukuba

edited by Lisa Lock, reviewed by Robert Egan

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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 maintaining the structural stability of tau filaments remains unclear.

For a new study published in Nature Structural & Molecular Biology, researchers from the University of Tsukuba extracted tau filaments from the brain tissue of patients with Alzheimer's disease and vacuolar tauopathy, a rare inherited neurodegenerative disease. They examined the filaments' biological and structural properties through mouse inoculation experiments and cryo-electron microscopy. Filaments from the two diseases produced distinct patterns of tau pathology in the mouse brain.

Cryo-electron microscopy also revealed that tau filament structures varied markedly between Alzheimer's disease and vacuolar tauopathy, with five distinct filament types identified in the latter. Shifting the position of polyubiquitin altered the interface between the two protofilaments in some tau filaments, leading to previously unobserved filament structures.

These results indicate that tau filament structure may be influenced not only by the highly ordered filament core but also by post-translational modifications surrounding it. The findings provide new insights into the mechanisms governing the formation and stabilization of disease-specific tau filament structures and may enhance our understanding of the structural diversity observed among tau-related neurodegenerative diseases.

Publication details

Ryohei Watanabe et al, Repositioning of polyubiquitin alters the pathologic tau filament structure, Nature Structural & Molecular Biology (2026). DOI: 10.1038/s41594-026-01879-4

Journal information: Nature Structural & Molecular Biology

Key medical concepts

Alzheimer's DiseaseCryoelectron Microscopy

Clinical categories

Neurology Provided by University of Tsukuba Who's behind this story?

Lisa Lock

BA art history, MA material culture. Former museum editor, paramedic, and transplant coordinator. Editing for Science X since 2021. Full profile →

Robert Egan

Bachelor's in mathematical biology, Master's in creative writing. Well-traveled with unique perspectives on science and language. Full profile →

Citation: Polyubiquitin may stabilize tau filament structures in neurodegenerative diseases (2026, October 4) retrieved 4 October 2026 from https://medicalxpress.com/news/2026-09-polyubiquitin-stabilize-tau-filament-neurodegenerative.html This document is subject to copyright. Apart from any fair dealing for the purpose of private study or research, no part may be reproduced without the written permission. The content is provided for information purposes only.