Tau aggregation
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Date
2026
Authors
Domene-Serrano, Indalo
Santa-María, Ismael
Hernandez, Felix
Avila, Jesús
Journal Title
Journal ISSN
Volume Title
Publisher
Universidad de Murcia, Departamento de Histología e Histopatología
Abstract
Microtubule-associated protein tau is predominantly expressed in neurons in the form of multiple isoforms generated by alternative splicing. These isoforms differ in the presence of either three or four microtubule-binding repeats. These binding regions not only regulate tau’s interaction with microtubules but are also critically involved in its pathological self-aggregation. Such aggregates are a defining feature of a group of neurodegenerative disorders collectively referred to as tauopathies.
In this work, we examine the mechanisms underlying tau self-aggregation, the molecular and cellular factors that drive this process, and the structural features of tau aggregates. Aggregates composed of isoforms with three versus four microtubule-binding repeats display distinct morphologies, which serve as pathological hallmarks for different tauopathies. Finally, we discuss potential therapeutic strategies aimed at preventing or promoting the clearance of tau aggregates.
Description
Keywords
Tau protein , Tau aggregation , Oligomer , Filaments , Regulatory factors
Citation
Histology and Histopathology, vol.41, nº2(2026)173-181
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